Cytochrome c 7: Difference between revisions

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==Structural Components==

Cc7 is a single polypeptide chain 68 residues total containing three heme groups. The polypeptide strand has one alpha helix 4 residues in length and two beta strands 2 residues in length. The heme groups are labelled as I, III, and IV. The binding site is located on the distal side of heme group IV where <scene name='71/716635/~~Active_site~~/1'>~~lysibe~~ residues 41, 42, 46 and 50</scene> are an interactive component of the active site. The net charge of these residues is positive, thus binding to negatively charge compounds or cations.<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>.

Cc7 is a single polypeptide chain 68 residues total containing three heme groups. The polypeptide strand has one alpha helix 4 residues in length and two beta strands 2 residues in length. The heme groups are labelled as I, III, and IV. The binding site is located on the distal side of heme group IV where <scene name='71/716635/Active_site_1/1'>lysine residues 41, 42, 46 and 50</scene> are an interactive component of the active site. The net charge of these residues is positive, thus binding to negatively charge compounds or cations.<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>.

== Function ==

Cytochrome c 7: Difference between revisions

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 ==Structural Components==
-Cc7 is a single polypeptide chain 68 residues total containing three heme groups. The polypeptide strand has one alpha helix 4 residues in length and two beta strands 2 residues in length. The heme groups are labelled as I, III, and IV. The binding site is located on the distal side of heme group IV where <scene name='71/716635/Active_site/1'>lysibe residues 41, 42, 46 and 50</scene> are an interactive component of the active site. The net charge of these residues is positive, thus binding to negatively charge compounds or cations.<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>.
+Cc7 is a single polypeptide chain 68 residues total containing three heme groups. The polypeptide strand has one alpha helix 4 residues in length and two beta strands 2 residues in length. The heme groups are labelled as I, III, and IV. The binding site is located on the distal side of heme group IV where <scene name='71/716635/Active_site_1/1'>lysine residues 41, 42, 46 and 50</scene> are an interactive component of the active site. The net charge of these residues is positive, thus binding to negatively charge compounds or cations.<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>.
 == Function ==