Journal of Biological Inorganic Chemistry最新文献

{"title":"Cobalt complexes in biology and medicine: enzymatic functions, pharmacological applications, and health challenges","authors":"Elham Motieiyan,&nbsp;Rasoul Motahari,&nbsp;Alireza Aliabadi,&nbsp;Samad Khaksar,&nbsp;Sara Abdolmaleki","doi":"10.1007/s00775-026-02149-w","DOIUrl":"10.1007/s00775-026-02149-w","url":null,"abstract":"<div><p>Cobalt is an essential trace element in biochemistry that plays a crucial role in the structure and function of several important biomolecules. In this review, vitamin B12 is discussed as one of the best-known examples in this area. Various forms of this vitamin, including methylcobalamin and adenosylcobalamin, play a crucial role in metabolic reactions in mammals and prokaryotes. It also discusses cobalt-containing enzymes that are essential for various biological processes. These enzymes are B12-dependent enzymes, which are well studied, and cobalt-containing enzymes, which are less well known, such as methionine aminopeptidase, nitrile hydratase, glucose isomerase, and prolidase. In addition to the significant role of cobalt complexes in biochemistry, these complexes are considered potent anticancer agents that can exert their antiproliferative effects through the production of ROS, cell cycle arrest, MMP breakdown, and induction of apoptosis in cancer cells. Cobalt complexes are also being explained here for their antimicrobial properties against a variety of pathogens, including bacteria, fungi, and viruses. Furthermore, examples of these complexes are presented as promising agents for the suppression of AD, which could be effective by binding to Aβ-peptides and preventing their aggregation, which is a central feature of the pathogenesis of AD, or by combating the oxidative damage associated with the disease, or even by interfering with the enzyme activities associated with this disease. Finally, the challenges related to the toxicity of cobalt and its compounds in medicine are discussed, and chelation therapy is considered an effective treatment for cobalt poisoning.</p></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 4","pages":"239 - 277"},"PeriodicalIF":2.8,"publicationDate":"2026-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147831785","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Immunoblot-based activity assay for heme-containing histidine kinases","authors":"Grant W. Larson,&nbsp;Eaindra Yee,&nbsp;Ambika Bhagi-Damodaran,&nbsp;Anoop Rama Damodaran","doi":"10.1007/s00775-026-02145-0","DOIUrl":"10.1007/s00775-026-02145-0","url":null,"abstract":"<div>\u0000 \u0000 <p>Histidine kinases (HKs) are essential bacterial signal transduction proteins and attractive drug targets due to their critical cellular functions. Direct measurement of their autophosphorylation activity is crucial for developing inhibitors and advancing disease treatments. While [γ-³²P]-ATP radiolabeling has long been a conventional method for kinase activity measurements, its reliance on ³²P introduces inherent limitations. The isotope’s short half-life imposes time-sensitive constraints on experiments, and stringent radiation safety and compliance requirements significantly increase operational costs. Several alternative methods including fluorescent phosphate-binding probes and fluorescence- or luminescence-based antibodies have been developed for HKs that overcome these challenges. However, for heme-based HKs, these alternatives are prone to interference from the luminescence of heme or fluorescence from a minor fraction of mismetalated Zn^II-bound protoporphyrin IX that is retained on the protein after gel electrophoresis. In this work, we address this interference by employing a near-IR (NIR) fluorophore-labeled secondary antibody and combining it with an ATPγS-utilizing immunoblot-based method to demonstrate ligation dependent thiophosphorylation activities of two heme-based HKs, DosS and GcHK. Consistent with previous studies, our NIR fluorescence-based immunoblot method reveals that GcHK is activated by ligand binding (O₂/CO), whereas the O₂-sensor DosS is inhibited upon binding O₂. Overall, this easy-to-implement method simplifies and democratizes activity measurements of heme-based HKs.</p>\u0000 </div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 on","pages":"163 - 171"},"PeriodicalIF":2.8,"publicationDate":"2026-04-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02145-0.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147759228","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Ag(I) complexes with natural products and triphenylphosphine: activity against tumor cell lines and mycobacterium tuberculosis","authors":"Jocely Lucena Dutra,&nbsp;João Honorato de Araujo-Neto,&nbsp;Rafael Wendel Rodrigues Santana,&nbsp;Rone Aparecido De Grandis,&nbsp;Giulia Polinário,&nbsp;Fernando Rogério Pavan,&nbsp;Javier Ellena,&nbsp;Alzir Azevedo Batista","doi":"10.1007/s00775-026-02144-1","DOIUrl":"10.1007/s00775-026-02144-1","url":null,"abstract":"<div>\u0000 \u0000 <p>Cancer and tuberculosis remain among the leading causes of morbidity and mortality worldwide, and the emergence of drug resistance in both diseases highlights the urgent need for new therapeutic strategies. In this context, metal-based compounds combined with bioactive natural products have emerged as promising alternatives to conventional drugs. In the present study, a series of silver (I) complexes containing natural products (curcumin, lawsone, lapachol or alizarin) and triphenylphosphine (PPh₃) (complexes <b>1</b>–<b>4</b>) were synthesized and structurally characterized by IR spectroscopy, elemental analysis, molar conductivity, NMR (¹H, ¹³C, ³¹P{¹H}) spectroscopy and single crystal X-ray diffraction. The results of single crystal diffraction show that the two silver complexes are four-coordinated with two PPh₃ and two O atoms of natural product, forming a distorted tetrahedral geometry. The in vitro cytotoxicity of silver(I) complexes was evaluated by MTT assay against four cancer cells and two normal cells, the result shows that the complexes presented a low IC₅₀ value in general, including in normal cell lines. The complexes show better cytotoxic activity for A2780cis (cisplatin-resistant ovarian tumor cell line), being nearly 30 times higher than cisplatin. Silver complexes were tested against Mycobacterium tuberculosis (Mtb) reaching the threshold for effective antimicrobial activity. Furthermore, complex <b>4</b> showed good activity against clinical isolates of Mtb resistant to multiple first-line anti-TB drugs.</p>\u0000 </div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 on","pages":"211 - 221"},"PeriodicalIF":2.8,"publicationDate":"2026-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02144-1.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147759215","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bovine xanthine oxidase electrocatalysis: substrate oxidation and its role in nitrite reduction","authors":"Peter D. Giang,&nbsp;Dimitri Niks,&nbsp;Russ Hille,&nbsp;Paul V. Bernhardt","doi":"10.1007/s00775-026-02146-z","DOIUrl":"10.1007/s00775-026-02146-z","url":null,"abstract":"<div><p>Xanthine oxidase plays a central role in purine catabolism in animals, plants and bacteria where it oxidises hypoxanthine to xanthine and xanthine to uric acid. In this work we have immobilised bovine xanthine oxidase on a glassy carbon electrode within a glutaraldehyde film and demonstrated hypoxanthine and xanthine oxidase electrocatalysis using mediator methylene blue as a mediator. The role of xanthine oxidase in the reduction of nitrite to nitric oxide has been probed in two ways. Using the electrochemically reduced mediator methyl viologen, nitrite reduction by xanthine oxidase is complicated by non-enzymatic reduction of nitrite by the mediator. Using hypoxanthine as reductant, nitrite reduction occurs but the product nitric oxide rapidly inactivates the enzyme. Xanthine oxidase can be restored to its functional form by redox cycling on an electrode in the presence of sulfide showing that nitric oxide leads to desulfuration of the molybdenum active site.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 on","pages":"145 - 151"},"PeriodicalIF":2.8,"publicationDate":"2026-04-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02146-z.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147759175","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The arsenic proteome in cancer: Unravelling molecular mechanisms of anticancer drugs","authors":"Hongyan Li,&nbsp;Hongzhe Sun","doi":"10.1007/s00775-026-02143-2","DOIUrl":"10.1007/s00775-026-02143-2","url":null,"abstract":"<div><p>Arsenic is a dual-natured element, functioning as both a carcinogen and a therapeutic agent in cancer treatment. Arsenic trioxide is a clinically approved drug for acute promyelocytic leukaemia, administered either alone or in combination with all-trans retinoic acid. Additionally, arsenic trioxide and organic arsenic compounds, such as darinaparsin, show promising efficacy against various cancers. Given the multi-targeted nature of metallodrugs, a comprehensive understanding of their molecular mechanisms is critical for the rational design of more potent and less toxic therapeutics. In this review, we first outline the structures and activities of key arsenic-based anticancer agents, encompassing both inorganic and organic forms. We then provide a comprehensive overview of proteome-wide identification of arsenic-binding proteins in cancer cells, utilizing metalloproteomic approaches such as immobilized metal affinity chromatography, continuous-flow electrophoresis coupled with inductively coupled plasma mass spectrometry, biotinylated arsenical pull-down, and fluorescence-based metalloproteomics. Subsequently, we discuss how the identified arsenic proteome facilitates elucidation of the molecular mechanisms of arsenic trioxide and darinaparsin from a systems perspective. We also evaluate studies on the cytotoxicity of arsenic compounds at the single-cell level, highlighting their role in improving our understanding of the mode of action of a drug. Finally, we prospect future research direction in this field. This review aims to stimulate further investigation into the molecular mechanisms of arsenic-based drugs at a systems level, guiding the development of more effective and safer arsenic-based therapeutics for cancer treatment.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 on","pages":"103 - 117"},"PeriodicalIF":2.8,"publicationDate":"2026-04-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02143-2.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147759252","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The evolutionary footprint of histidine in hemoglobin and myoglobin: an implication towards their function","authors":"Jayraj Biswas,&nbsp;Kauseki Dutta,&nbsp;Kakali Biswas,&nbsp;Raja Banerjee","doi":"10.1007/s00775-026-02147-y","DOIUrl":"10.1007/s00775-026-02147-y","url":null,"abstract":"<div><p>Hemoglobin and myoglobin are essential oxygen-binding proteins whose structural integrity is critical for proper function. This study performs atomic-level comparisons of wild-type and mutant forms to investigate how specific mutations impact oxygen-binding affinity. Substitution of the proximal histidine, responsible for coordinating the iron atom in the heme group, with tyrosine results shortening of bond distances in haemoglobin, while Van der Waals clashes in myoglobin; impairing function of both. Other mutations (α125Leu &gt; Pro, β34Val &gt; Asp, β63His &gt; Tyr, β92His &gt; Asn) compromise the protein stability by disrupting inter-chain hydrogen bonds and helical structures, reducing oxygen-binding efficiency. Cross-species comparisons, from <i>Actinopterygii</i> to <i>Mammalia</i>, underscore strong conservation of these critical residues essential for preserving the indispensable structural and functional integrity of these proteins since the dawn of their existence.</p><h3>Graphical abstract</h3><p>Since the dawn of its existence high conservation of sequences especially histidine for maintaining the functionality of hemoglobin and myoglobin.</p><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 on","pages":"223 - 238"},"PeriodicalIF":2.8,"publicationDate":"2026-04-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147669785","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"[FeFe] hydrogenases with modified azadithiolate bridgeheads serve as unidirectional hydrogen oxidation catalysts","authors":"Manon T. Lachmann,&nbsp;James A. Birrell,&nbsp;Simone Morra,&nbsp;Patricia Rodríguez-Maciá","doi":"10.1007/s00775-026-02141-4","DOIUrl":"10.1007/s00775-026-02141-4","url":null,"abstract":"<div><p>Semi-synthetic [FeFe] hydrogenases hold exciting potential as tuneable artificial metalloenzymes for efficient hydrogen conversion (H₂ <span>(rightleftharpoons)</span> 2 H⁺ + 2e⁻). This work investigates the role of the bridgehead ligand in the [FeFe] hydrogenase active site through the study of two bridgehead-modified active-site variants (2-oxapropane 1,3-dithiolate, ODT, and propane 1,3-dithiolate, PDT). Replacing the native 2-azapropane 1,3-dithiolate (ADT) bridgehead with ODT or PDT significantly modifies the active site’s electronic structure and disrupts proton-transfer; yet, some catalytic activity remains, suggesting that alternative catalytic pathways may exist. Notably, when adsorbed onto an electrode, the ODT enzymes operate as proficient catalysts for hydrogen oxidation at higher oxidative overpotentials, achieving current densities of up to 1 mA cm^− 2, comparable to those observed for the respective ADT enzyme under the same conditions. Electrochemical analysis reveals similar catalytic behaviour between the ODT and PDT enzymes, suggesting that a proton transfer pathway between the active site and the protein environment still operates, albeit disrupted, in both bridgehead variants under these conditions. Insights into the electronic and catalytic interplay of these modifications could advance the optimisation of semi-synthetic [FeFe] hydrogenases and design of new bioinspired catalysts.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 on","pages":"131 - 144"},"PeriodicalIF":2.8,"publicationDate":"2026-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02141-4.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147615627","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Role of the NHE1 exchanger in the antitumor effects of copper(II) complexes and phenanthroline derivatives","authors":"K. S. Muñoz Garzón,&nbsp;V. Martínez,&nbsp;V. de Giusti,&nbsp;D. Pérez Visñuk,&nbsp;M. Villaverde,&nbsp;N. Alvarez,&nbsp;G. Facchin,&nbsp;A. L. Di Virgilio","doi":"10.1007/s00775-026-02142-3","DOIUrl":"10.1007/s00775-026-02142-3","url":null,"abstract":"<div>\u0000 \u0000 <p>Three copper(II) complexes containing 1,10-phenanthroline: [CuCl₂(phen)]·0.5H₂O (<b>1</b>), neocuproine [CuCl₂(neo)]·0.75 H₂O (<b>2</b>) and tetramethyl-phenanthroline [CuCl₂(tmp)]·H₂O (<b>3</b>) as the primary ligand and another three copper(II) complexes with L-Ala-Phe dipeptide as auxiliary ligand: [Cu(L-Ala-Phe)(phen)]·4H₂O (<b>4</b>), [Cu(L-Ala-Phe)(neo)]·3H₂O (<b>5</b>) and [Cu(L-Ala-Phe)(tmp)]·3H₂O (<b>6</b>), inhibited cell viability in the MCF-7 cell line, both in the monolayer and spheroid models. The pair with tmp displayed a better selectivity index than cisPt and non-cytotoxicity-related ROS induction and apoptosis in the monolayer model. Cell proliferation was affected by all compounds in a concentration-dependent manner. Cell viability on spheroids showed a reduction from 1 µM, with IC₅₀ values that were half those of cisplatin. All copper complexes, except for <b>1</b>, showed DNA damage at a concentration below IC₅₀. Our study revealed that all compounds inhibited sodium-hydrogen exchanger (NHE1) activity in MCF-7 cells. However, only complexes containing the dipeptide could extend their effect on cell migration and metalloprotease MMP-9 activity. Western Blot analysis showed that metalloproteases MMP-2, MMP-9, and NHE1 expression was also affected when MCF-7 cells were treated with the six compounds. Overall, our results reveal an antitumor effect of all copper(II) complexes studied in breast cancer cells and a fundamental role of NHE1 in cell migration.</p>\u0000 </div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 on","pages":"193 - 209"},"PeriodicalIF":2.8,"publicationDate":"2026-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147493387","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Lessons, connections, hypotheses and predictions from protein film electrochemistry","authors":"Fraser A. Armstrong","doi":"10.1007/s00775-026-02136-1","DOIUrl":"10.1007/s00775-026-02136-1","url":null,"abstract":"<div><p>This extended essay describes the development of protein film electrochemistry (PFE) as a powerful suite of techniques for investigating how electron-transfer processes occurring in biological molecules are coupled to chemical reactions. Based on the author’s personal experiences, the article explores the wider picture through connections to related work and other scientific areas, as well as hypotheses and predictions. Extending far beyond its electrochemical origins and early expectations, PFE has reached a wide audience – across disciplines as diverse as electrochemistry, renewable energy, biological coordination chemistry, molecular catalysis, biocatalysis, molecular and cell biology, biotechnology and pharmacology. Much is owed to many researchers, from undergraduates to senior figures, with whom the author has worked alongside and been inspired by for more than 40 years.</p><h3>Graphical abstract</h3><div><figure><div><div><picture><source><img></source></picture><span>The alternative text for this image may have been generated using AI.</span></div></div></figure></div></div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 1-2","pages":"1 - 28"},"PeriodicalIF":2.7,"publicationDate":"2026-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02136-1.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147430088","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A bioinorganic view on the potential chemical space of hydroxyphenylpyruvate dioxygenase-like (HPDL) enzymes","authors":"Niko S. W. Lindlar,&nbsp;Rolf Stucka,&nbsp;Sophie M. Gutenthaler-Tietze,&nbsp;Jonathan Gutenthaler-Tietze,&nbsp;Jan Senderek,&nbsp;Lena J. Daumann","doi":"10.1007/s00775-026-02137-0","DOIUrl":"10.1007/s00775-026-02137-0","url":null,"abstract":"<div>\u0000 \u0000 <p>Genetic analyses have identified biallelic variants in the <i>4-hydroxyphenylpyruvate dioxygenase-like</i> (<i>HPDL</i>) gene as the cause of a neurodegenerative disease that resembles the primary coenzyme Q10 (CoQ10) deficiency syndromes. HPDL is structurally similar to the well-studied 4-hydroxyphenyl pyruvate dioxygenase (HPPD), an iron(II)/α-ketoacid-dependent enzyme. HPPD is known to catalyze the second step in the tyrosine metabolism, the oxidative conversion of 4-hydroxyphenylpyruvate (4-HPP) to homogentisic acid (HGA). Hereditary HPPD deficiencies result in high blood tyrosine levels (tyrosinemia type III), which are associated with neurological symptoms such as mental retardation and ataxia. In 2021, 4-hydroxymandelate (4-HMA) was identified as the long-sought intermediate of the biosynthetic pathway from tyrosine to CoQ10. CoQ10 is an important electron shuttle needed in mitochondria for ATP production. Interestingly, HPDL was shown to be able to catalyze the oxygen-dependent reaction of 4-HPP to 4-HMA. Both 4-HPA and 4-HBz occur in the CoQ10 biosynthetic pathway of mammals. CoQ10 has been suspected to be necessary for correct neuronal function, a link to the neurodegenerative HPDL variants. Here, we present a bioinorganic model that can mimic this potential role of HPDL in the conversion of 4-hydroxyphenylpyruvic acid (4-HPA) to 4-hydroxybenzaldehyde (4-HBz). We used fully synthetic iron(III)-hydroxido and iron(IV)-oxido complexes with a ligand of the pentapyridyl-type to study the interconversion of 4-HPA to 4-HBz from a bioinorganic point of view. We show that while an iron(IV)-oxido species, as it occurs in HPPD, is capable of performing the first reaction step from 4-HPA to 4-HMA, an iron(III)-hydroxido species is capable of the transformation of 4-HMA to 4-HBz.</p>\u0000 </div>","PeriodicalId":603,"journal":{"name":"Journal of Biological Inorganic Chemistry","volume":"31 1-2","pages":"91 - 99"},"PeriodicalIF":2.7,"publicationDate":"2026-03-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s00775-026-02137-0.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147430067","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}