Advances in inorganic biochemistry最新文献

{"title":"The metallothionein structural motif in gene expression.","authors":"D R Winge,&nbsp;C T Dameron,&nbsp;G N George","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Metalloregulation in eukaryotic organisms is poorly understood. Only a limited number of physiological processes are currently known to be regulated by metal ions. Copper salts stimulate transcription of MT and SOD genes in fungi and repress expression of cytochrome c6 in algae. The Cu-activation of gene expression in fungi is mediated by a Cu1+ specific sensor protein. The mechanism of Cu-activation of the sensor molecule, ACE1 (and probably AMT1), appears to be the formation of a CuS polymetallic cluster as the structural core of the proteins. Structural similarities between ACE1, AMT1 and metallothionein suggest that the MT motif is a good structural model to explain the metal-specific activation and specificity of the two signal transducing proteins. Metal ion specificity is achieved by the propensity of proteins with a MT motif to form multinuclear CuS centers. Coordination inorganic chemistry appears to be the driving force for Cu1+ metalloregulation in biology. The metalloregulation of transcriptional activation of mammalian MT genes will be intriguing as metal ion selectivity is not as apparent. The MT motif is not expected to be a highly redundant structural theme. The intriguing observation by Uchida et al. (154) that the growth inhibitory factor (MTIII) deficient in the brains of Alzheimer's patients is homologous to metallothioneins raises the likelihood that coordination chemistry will be critical in stabilizing the bioactive form of MTIII. The motif may be observed in yet to be identified metalloregulatory proteins that regulate other processes in a Cu- or Zn-specific manner. Formation of metal:thiolate polymetallic clusters allows a significant volume of the protein structure to be altered, so metal-induced structural dynamics are possible. CuS polynuclear clusters may be more general than the MT motif in biology. The only molecules currently known to form CuS polynuclear clusters include MT, ACE1 and the Cu(gamma EC)nG complexes, although AMT1 and MTIII are expected to be the next members in the list. Three other Cys-rich proteins, papilloma viral E7 and LIM motif-containing CRP and CRIP, isolated as Zn2+ proteins exhibit facile metal exchange in vitro with Cu1+. The resulting Cu1+ proteins show optical properties similar to CuMTs (202,203). Although CuS clusters may form in E7 and LIM-containing proteins, it is premature to ascribe any biological significance to the Cu1+ conformers.</p>","PeriodicalId":77659,"journal":{"name":"Advances in inorganic biochemistry","volume":"10 ","pages":"1-48"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19193038","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A ribozyme model: site-specific cleavage of an RNA substrate by Mn2+.","authors":"R B Van Atta,&nbsp;S M Hecht","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77659,"journal":{"name":"Advances in inorganic biochemistry","volume":"9 ","pages":"1-40"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"18519503","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Insights into the structural and electronic properties of metalloproteins by heteronuclear magnetic resonance.","authors":"P R Blake,&nbsp;M F Summers","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77659,"journal":{"name":"Advances in inorganic biochemistry","volume":"10 ","pages":"201-28"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19193043","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cytochrome P-450 and peroxidase chemistry.","authors":"J E Erman,&nbsp;L P Hager,&nbsp;S G Sligar","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77659,"journal":{"name":"Advances in inorganic biochemistry","volume":"10 ","pages":"71-118"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19193044","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Selenium biochemistry--selected topics.","authors":"T C Stadtman","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77659,"journal":{"name":"Advances in inorganic biochemistry","volume":"10 ","pages":"157-75"},"PeriodicalIF":0.0,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19193041","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Regulation of metallothionein gene transcription by metals.","authors":"J Imbert,&nbsp;V Culotta,&nbsp;P Fürst,&nbsp;L Gedamu,&nbsp;D Hamer","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77659,"journal":{"name":"Advances in inorganic biochemistry","volume":"8 ","pages":"139-64"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13358987","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Alternative nitrogenase.","authors":"B J Hales","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Recently, it has been demonstrated that both A. vinelandii and A. chroococcum have the ability to synthesize several different nitrogen-fixing enzymes. Both species can produce a Mo- or V-containing nitrogenase while A. vinelandii can also generate an all-Fe form of the enzyme. Regardless of the source or form of the enzyme, all nitrogenases are composed of two separable proteins, called components 1 and 2, where component 2 is a highly conserved dimer containing a single [4Fe-4S] cluster. The major differences among the various forms of the enzyme are in component 1, the protein where substrate reduction occurs. This protein can exist in forms of four, five, or six subunits and can contain Mo, V or only Fe at the putative active site. Finally, there are also variations among the different enzyme systems regarding the paramagnetism of component 1 as well as the general substrate reduction patterns. While it is not yet known why these bacteria possess the ability to generate multiple forms of nitrogenase or which form of the enzyme has the greatest physiological importance, the existence of these various nitrogenases raises several other important questions. Specifically, how do Mo, V and Fe regulate the synthesis of each enzyme system, which genes are unique and which are common for these systems, and what roles, if any, do Mo, V and Fe play in catalysis? The fact that we can now use three different enzyme systems to investigate nitrogen fixation may greatly increase our ability to answer these questions and eventually understand the mechanism of this very important enzymatic reaction.</p>","PeriodicalId":77659,"journal":{"name":"Advances in inorganic biochemistry","volume":"8 ","pages":"165-98"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13358988","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Regulation of ferritin gene expression.","authors":"R S Eisenstein,&nbsp;A J Bettany,&nbsp;H N Munro","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77659,"journal":{"name":"Advances in inorganic biochemistry","volume":"8 ","pages":"91-138"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13358991","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Regulation of gene expression by mercury.","authors":"J D Helmann,&nbsp;L M Shewchuk,&nbsp;C T Walsh","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77659,"journal":{"name":"Advances in inorganic biochemistry","volume":"8 ","pages":"33-61"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13358989","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular aspects of regulation of high affinity iron absorption in microorganisms.","authors":"J B Neilands","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77659,"journal":{"name":"Advances in inorganic biochemistry","volume":"8 ","pages":"63-90"},"PeriodicalIF":0.0,"publicationDate":"1990-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"13358990","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}