Literature DB >> 7880886

The protein moiety modulates the redox potential in cytochromes c.

A Dolla1, L Blanchard, F Guerlesquin, M Bruschi.   

Abstract

Cytochrome c is one of the most thoroughly documented oxidoreduction proteins. Its electron transfer activity, which involves an association between the heme group and the polypeptidic chain, is correlated with the redox potential value of the heme group. The redox potential covers a wide range up to 0.8 V, an extreme case being observed in the low-potential cytochromes c from sulfate reducing bacteria. On of the main roles of the polypeptidic moiety consists of modulating the redox potential value of the heme group. In this paper, some structural factors that seem likely to be involved in maintaining the redox potential value are described.

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Year:  1994        PMID： 7880886     DOI： 10.1016/0300-9084(94)90171-6

Source DB:  PubMed          Journal:  Biochimie        ISSN： 0300-9084            Impact factor:   4.079


  8 in total

1.  Thermodynamic characterization of a tetrahaem cytochrome isolated from a facultative aerobic bacterium, Shewanella frigidimarina: a putative redox model for flavocytochrome c3.

Authors:  Miguel Pessanha; Ricardo O Louro; Ilídio J Correia; Emma L Rothery; Kate L Pankhurst; Graeme A Reid; Stephen K Chapman; David L Turner; Carlos A Salgueiro
Journal:  Biochem J       Date:  2003-03-01       Impact factor: 3.857

2.  Positive selection on the killer whale mitogenome.

Authors:  Andrew D Foote; Phillip A Morin; John W Durban; Robert L Pitman; Paul Wade; Eske Willerslev; M Thomas P Gilbert; Rute R da Fonseca
Journal:  Biol Lett       Date:  2010-09-01       Impact factor: 3.703

3.  Electric-field-induced redox potential shifts of tetraheme cytochromes c3 immobilized on self-assembled monolayers: surface-enhanced resonance Raman spectroscopy and simulation studies.

Authors:  Laura Rivas; Cláudio M Soares; António M Baptista; Jalila Simaan; Roberto E Di Paolo; Daniel H Murgida; Peter Hildebrandt
Journal:  Biophys J       Date:  2005-03-11       Impact factor: 4.033

4.  Dissection of hydrogen bond interaction network around an iron-sulfur cluster by site-specific isotope labeling of hyperthermophilic archaeal Rieske-type ferredoxin.

Authors:  Toshio Iwasaki; Risako Fukazawa; Yoshiharu Miyajima-Nakano; Amgalanbaatar Baldansuren; Shinichi Matsushita; Myat T Lin; Robert B Gennis; Kazuya Hasegawa; Takashi Kumasaka; Sergei A Dikanov
Journal:  J Am Chem Soc       Date:  2012-11-20       Impact factor: 15.419

5.  Catalytic Reactions and Energy Conservation in the Cytochrome bc1 and b6f Complexes of Energy-Transducing Membranes.

Authors:  Marcin Sarewicz; Sebastian Pintscher; Rafał Pietras; Arkadiusz Borek; Łukasz Bujnowicz; Guy Hanke; William A Cramer; Giovanni Finazzi; Artur Osyczka
Journal:  Chem Rev       Date:  2021-01-19       Impact factor: 60.622

6.  Cloning and sequence of cymA, a gene encoding a tetraheme cytochrome c required for reduction of iron(III), fumarate, and nitrate by Shewanella putrefaciens MR-1.

Authors:  C R Myers; J M Myers
Journal:  J Bacteriol       Date:  1997-02       Impact factor: 3.490

7.  The tetraheme cytochrome from Shewanella oneidensis MR-1 shows thermodynamic bias for functional specificity of the hemes.

Authors:  Bruno M Fonseca; Ivo H Saraiva; Catarina M Paquete; Claudio M Soares; Isabel Pacheco; Carlos A Salgueiro; Ricardo O Louro
Journal:  J Biol Inorg Chem       Date:  2008-12-02       Impact factor: 3.358

8.  Structure of a novel c7-type three-heme cytochrome domain from a multidomain cytochrome c polymer.

Authors:  P Raj Pokkuluri; Yuri Y Londer; Norma E C Duke; Jill Erickson; Miguel Pessanha; Carlos A Salgueiro; Marianne Schiffer
Journal:  Protein Sci       Date:  2004-05-07       Impact factor: 6.725
  8 in total

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