Literature DB >> 208660

EPR determination of the oxidation-reduction potentials of the hemes in cytochrome c3 from Desulfovibrio vulgaris.

D V Dervartanian, A V Xavier, J L Gall.   

Abstract

EPR spectroscopy in conjunction with oxidation-reduction potentiometry has been used to determine the half-reduction potentials of the four hemes of cytochrome c3. As predicted, the four hemes of cytochrome c3 have different mid-point potentials. The Em values are: Heme I,--284 mV; Heme II,--310 mV; Heme III,--324 mV and Heme IV,--319 mV. The n-values in each case was near one.

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Year:  1978        PMID: 208660     DOI: 10.1016/s0300-9084(78)80829-3

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


  4 in total

Review 1.  Proton thrusters: overview of the structural and functional features of soluble tetrahaem cytochromes c3.

Authors:  Ricardo O Louro
Journal:  J Biol Inorg Chem       Date:  2006-09-09       Impact factor: 3.358

2.  Factors influencing redox potentials of electron transfer proteins.

Authors:  G R Moore; G W Pettigrew; N K Rogers
Journal:  Proc Natl Acad Sci U S A       Date:  1986-07       Impact factor: 11.205

3.  Characterization of cytochrome c3 from the thermophilic sulfate reducer Thermodesulfobacterium commune.

Authors:  E C Hatchikian; P Papavassiliou; P Bianco; J Haladjian
Journal:  J Bacteriol       Date:  1984-09       Impact factor: 3.490

4.  A periplasmic and extracellular c-type cytochrome of Geobacter sulfurreducens acts as a ferric iron reductase and as an electron carrier to other acceptors or to partner bacteria.

Authors:  S Seeliger; R Cord-Ruwisch; B Schink
Journal:  J Bacteriol       Date:  1998-07       Impact factor: 3.490

  4 in total

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