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1ofw

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{{STRUCTURE_1ofw| PDB=1ofw | SCENE= }}
{{STRUCTURE_1ofw| PDB=1ofw | SCENE= }}
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'''THREE DIMENSIONAL STRUCTURE OF THE OXIDIZED FORM OF NINE HEME CYTOCHROME C AT PH 7.5'''
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===THREE DIMENSIONAL STRUCTURE OF THE OXIDIZED FORM OF NINE HEME CYTOCHROME C AT PH 7.5===
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==Overview==
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The nine-heme cytochrome c is a monomeric multiheme cytochrome found in Desulfovibrio desulfuricans ATCC 27774. The polypeptide chain comprises 296 residues and wraps around nine hemes of type c. It is believed to take part in the periplasmic assembly of proteins involved in the mechanism of hydrogen cycling, receiving electrons from the tetraheme cytochrome c3. With the purpose of understanding the molecular basis of electron transfer processes in this cytochrome, we have determined the crystal structures of its oxidized and reduced forms at pH 7.5 and performed theoretical calculations of the binding equilibrium of protons and electrons in these structures. This integrated study allowed us to observe that the reduction process induced relevant conformational changes in several residues, as well as protonation changes in some protonatable residues. In particular, the surroundings of hemes I and IV constitute two areas of special interest. In addition, we were able to ascertain the groups involved in the redox-Bohr effect present in this cytochrome and the conformational changes that may underlie the redox-cooperativity effects on different hemes. Furthermore, the thermodynamic simulations provide evidence that the N- and C-terminal domains function in an independent manner, with the hemes belonging to the N-terminal domain showing, in general, a lower redox potential than those found in the C-terminal domain. In this way, electrons captured by the N-terminal domain could easily flow to the C-terminal domain, allowing the former to capture more electrons. A notable exception is heme IX, which has low redox potential and could serve as the exit path for electrons toward other proteins in the electron transfer pathway.
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(as it appears on PubMed at http://www.pubmed.gov), where 12750363 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12750363}}
==About this Structure==
==About this Structure==
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[[Category: Electron transpor]]
[[Category: Electron transpor]]
[[Category: Multiheme cytochrome c]]
[[Category: Multiheme cytochrome c]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:10:00 2008''

Revision as of 05:10, 28 July 2008

Image:1ofw.png

Template:STRUCTURE 1ofw

THREE DIMENSIONAL STRUCTURE OF THE OXIDIZED FORM OF NINE HEME CYTOCHROME C AT PH 7.5

Template:ABSTRACT PUBMED 12750363

About this Structure

1OFW is a Single protein structure of sequence from Desulfovibrio desulfuricans. Full crystallographic information is available from OCA.

Reference

Redox-Bohr and other cooperativity effects in the nine-heme cytochrome C from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies., Bento I, Teixeira VH, Baptista AM, Soares CM, Matias PM, Carrondo MA, J Biol Chem. 2003 Sep 19;278(38):36455-69. Epub 2003 May 15. PMID:12750363

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