{"title":"Magnetic relaxometry of methemoglobin by widefield nitrogen-vacancy microscopy","authors":"Suvechhya Lamichhane, Evelyn Carreto Guevara, Ilja Fescenko, Sy-Hwang Liou, Rebecca Y. Lai, Abdelghani Laraoui","doi":"10.1063/5.0217987","DOIUrl":null,"url":null,"abstract":"Hemoglobin (Hb) is a multifaceted protein, classified as a metalloprotein, chromoprotein, and globulin. It incorporates iron, which plays a crucial role in transporting oxygen within red blood cells. Hb functions by carrying oxygen from the respiratory organs to diverse tissues in the body, where it releases oxygen to fuel aerobic respiration, thus supporting the organism's metabolic processes. Hb can exist in several forms, primarily distinguished by the oxidation state of the iron in the heme group, including methemoglobin (MetHb). Measuring the concentration of MetHb is crucial because it cannot transport oxygen; hence, higher concentrations of MetHb in the blood causes methemoglobinemia. Here, we use optically detected magnetic relaxometry of paramagnetic iron spins in MetHb drop-cast onto a nanostructured diamond doped with shallow high-density nitrogen-vacancy (NV) spin qubits. We vary the concentration of MetHb in the range of 6 × 106–1.8 × 107 adsorbed Fe+3 spins per micrometer squared and observe an increase in the NV relaxation rate Γ1 (=1/T1, where T1 is the NV spin lattice relaxation time) up to 2 × 103 s−1. NV magnetic relaxometry of MetHb in phosphate-buffered saline solution shows a similar effect with an increase in Γ1 to 6.7 × 103 s−1 upon increasing the MetHb concentration to 100 μM. The increase in NV Γ1 is explained by the increased spin noise coming from the Fe+3 spins present in MetHb proteins. This study presents an additional usage of NV quantum sensors to detect paramagnetic centers of biomolecules at volumes below 100 picoliter.","PeriodicalId":8094,"journal":{"name":"Applied Physics Letters","volume":null,"pages":null},"PeriodicalIF":3.5000,"publicationDate":"2024-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Applied Physics Letters","FirstCategoryId":"101","ListUrlMain":"https://doi.org/10.1063/5.0217987","RegionNum":2,"RegionCategory":"物理与天体物理","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"PHYSICS, APPLIED","Score":null,"Total":0}
引用次数: 0
Abstract
Hemoglobin (Hb) is a multifaceted protein, classified as a metalloprotein, chromoprotein, and globulin. It incorporates iron, which plays a crucial role in transporting oxygen within red blood cells. Hb functions by carrying oxygen from the respiratory organs to diverse tissues in the body, where it releases oxygen to fuel aerobic respiration, thus supporting the organism's metabolic processes. Hb can exist in several forms, primarily distinguished by the oxidation state of the iron in the heme group, including methemoglobin (MetHb). Measuring the concentration of MetHb is crucial because it cannot transport oxygen; hence, higher concentrations of MetHb in the blood causes methemoglobinemia. Here, we use optically detected magnetic relaxometry of paramagnetic iron spins in MetHb drop-cast onto a nanostructured diamond doped with shallow high-density nitrogen-vacancy (NV) spin qubits. We vary the concentration of MetHb in the range of 6 × 106–1.8 × 107 adsorbed Fe+3 spins per micrometer squared and observe an increase in the NV relaxation rate Γ1 (=1/T1, where T1 is the NV spin lattice relaxation time) up to 2 × 103 s−1. NV magnetic relaxometry of MetHb in phosphate-buffered saline solution shows a similar effect with an increase in Γ1 to 6.7 × 103 s−1 upon increasing the MetHb concentration to 100 μM. The increase in NV Γ1 is explained by the increased spin noise coming from the Fe+3 spins present in MetHb proteins. This study presents an additional usage of NV quantum sensors to detect paramagnetic centers of biomolecules at volumes below 100 picoliter.
期刊介绍:
Applied Physics Letters (APL) features concise, up-to-date reports on significant new findings in applied physics. Emphasizing rapid dissemination of key data and new physical insights, APL offers prompt publication of new experimental and theoretical papers reporting applications of physics phenomena to all branches of science, engineering, and modern technology.
In addition to regular articles, the journal also publishes invited Fast Track, Perspectives, and in-depth Editorials which report on cutting-edge areas in applied physics.
APL Perspectives are forward-looking invited letters which highlight recent developments or discoveries. Emphasis is placed on very recent developments, potentially disruptive technologies, open questions and possible solutions. They also include a mini-roadmap detailing where the community should direct efforts in order for the phenomena to be viable for application and the challenges associated with meeting that performance threshold. Perspectives are characterized by personal viewpoints and opinions of recognized experts in the field.
Fast Track articles are invited original research articles that report results that are particularly novel and important or provide a significant advancement in an emerging field. Because of the urgency and scientific importance of the work, the peer review process is accelerated. If, during the review process, it becomes apparent that the paper does not meet the Fast Track criterion, it is returned to a normal track.