Cytochrome c 7: Difference between revisions

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Alexander Douglas, Michal Harel, Alexander Berchansky

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 <StructureSection load='1LM2.pdb' size='340' side='right' caption='3D Structure of Cytochrome c 7' scene=''>
-'''Cytocrhome c 7''' (Cc7) is a three heme-containing protein derived from the sulfur-reducing bacterium ''Desulfuromonas acetoxidans''. Cc7 is located in the mitochondrial intermembrane space of the bacteria where it plays a role in the electron-transfer mechanism <ref>Assfalg M, Bertini I, Bruschi M, Michel C, Turano P. The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c(7). 2002; 99(15):9750-4 '''[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC125002/''' DOI: 10.1073/pnas.152290999''']'''</ref>. ''Desulfuromonas acetoxidans'' bacteria have evolved to obtain their energy from anaerobic sulfure respiration, thus requiring organic disulfide compounds as electron acceptors<ref>Pfennig N, Biebl H. Desulfuromonas acetoxidans gen. nov. and sp. nov., a new anaerobic, sulfur-reducing, acetate-oxidizing bacterium. 1976; 110(1): 3-12. DOI: 10.1007/BF00416962</ref>.
+'''Cytocrhome c 7''' (Cc7) is a three heme-containing protein derived from the sulfur-reducing bacterium ''Desulfuromonas acetoxidans''. Cc7 is located in the mitochondrial intermembrane space of the bacteria where it plays a role in the electron-transfer mechanism <ref>Assfalg M, Bertini I, Bruschi M, Michel C, Turano P. The metal reductase activity of some multiheme cytochromes c: NMR structural characterization of the reduction of chromium(VI) to chromium(III) by cytochrome c(7). 2002; 99(15):9750-4 '''[http://www.ncbi.nlm.nih.gov/pmc/articles/PMC125002/''' DOI: 10.1073/pnas.152290999''']'''</ref>. ''Desulfuromonas acetoxidans'' bacteria have evolved to obtain their energy from anaerobic sulfure respiration, thus requiring organic disulfide compounds, such as thiosulfate, sulfur, sulfite, or sulfate, as their electron acceptors<ref>Pfennig N, Biebl H. Desulfuromonas acetoxidans gen. nov. and sp. nov., a new anaerobic, sulfur-reducing, acetate-oxidizing bacterium. 1976; 110(1): 3-12 '''[http://link.springer.com/article/10.1007/BF00416962''' DOI: 10.1007/BF00416962''']'''</ref>. This gives Cc7 a very unique ability that interests a lot of researchers as of late: the fact that this protein is able to reduce disulfide compounds down to hydrogen sulfide, which in turn reacts with heavy metal ions to form low-toxicity metal sulfides<ref>Pfennig N, Biebl H. Desulfuromonas acetoxidans gen. nov. and sp. nov., a new anaerobic, sulfur-reducing, acetate-oxidizing bacterium. 1976; 110(1): 3-12 '''[http://link.springer.com/article/10.1007/BF00416962''' DOI: 10.1007/BF00416962''']'''</ref>. To apply this characteristic, researchers hope to create possible applications to use these bacteria in decontamination of environments that are polluted with toxic heavy metals. Because of the insolubility of the metal sulfides, removing them from the environment will be simpler and cheaper than current heavy metal toxic waste filtration operations<ref>National Service Center for Environmental Publications. [http://nepis.epa.gov/Exe/ZyNET.exe/91018HWZ.txt?ZyActionD=ZyDocument&Client=EPA&Index=1976%20Thru%201980&Docs=&Query=&Time=&EndTime=&SearchMethod=1&TocRestrict=n&Toc=&TocEntry=&QField=&QFieldYear=&QFieldMonth=&QFieldDay=&UseQField=&IntQFieldOp=0&ExtQFieldOp=0&XmlQuery=&File=D%3A\ZYFILES\INDEX%20DATA\76THRU80\TXT\00000025\91018HWZ.txt&User=ANONYMOUS&Password=anonymous&SortMethod=h|-&MaximumDocuments=1&FuzzyDegree=0&ImageQuality=r75g8/r75g8/x150y150g16/i425&Display=p|f&DefSeekPage=x&SearchBack=ZyActionL&Back=ZyActionS&BackDesc=Results%20page&MaximumPages=1&ZyEntry=1]</ref>.
 ==Structural Components==
+Cc7 is a single polypeptide chain 68 residues long containing three heme groups. The polypeptide strand has one alpha helix 4 residues long and two beta sheet 2 residues)
 == Function ==