Crystallographic studies of cytochrome c and cytochrome c oxidase [PDF]
The Journal of Biochemistry, 2021 I started on crystallographic studies of cytochrome c (Cyt.c) in the later 1960s at Institute for Protein Research, Osaka University. The institute successfully built the structural model of ferro-Cyt.c by the multiple heavy atom replacement method in the early 1970s.
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Biogenesis of mitochondrial c-type cytochromes [PDF]
, 1990 Cytochromesc andc 1 are essential components of the mitochondrial respiratory chain. In both cytochromes the heme group is covalently linked to the polypeptide chain via thioether bridges. The location of the two cytochromes is in the intermembrane space;
Gonzales, Daniel H., Neupert, Walter
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A dedicated haem lyase is required for the maturation of a novel bacterial cytochrome c with unconventional covalent haem binding [PDF]
, 2007 In bacterial c-type cytochromes, the haem cofactor is covalently attached via two cysteine residues organized in a haem c-binding motif. Here, a novel octa-haem c protein, MccA, is described that contains only seven conventional haem c-binding motifs ...
Allen J.W.A. +17 more
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Sampling Field Heterogeneity at the Heme of c-Type Cytochromes by Spectral Hole Burning Spectroscopy and Electrostatic Calculations [PDF]
, 1999 We report on a comparative investigation of the heme pocket fields of two Zn-substituted c-type cytochromes—namely yeast and horse heart cytochromes c—using a combination of hole burning Stark spectroscopy and electrostatic calculations.
Friedrich, Josef +3 more
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Functional and Biogenetical Heterogeneity of the Inner Membrane of Rat-Liver Mitochondria [PDF]
, 1971 Rat liver mitochondria were fragmented by a combined technique of swelling, shrinking, and sonication. Fragments of inner membrane were separated by density gradient centrifugation.
Allmann D. W. +50 more
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Cytochrome c and superoxide [PDF]
JBIC Journal of Biological Inorganic Chemistry, 2013 ISSN:0949 ...
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Biochemical requirements for the maturation of mitochondrial c-type cytochromes [PDF]
, 2009 Cytochromes c are metalloproteins that function in electron transfer reactions and contain a heme moiety covalently attached via thioether linkages between the co-factor and a CXXCH motif in the protein.
Bonnard, Géraldine +3 more
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Mechanisms of Bacterial Extracellular Electron Exchange. [PDF]
, 2016 The biochemical mechanisms by which microbes interact with extracellular soluble metal ions and insoluble redox-active minerals have been the focus of intense research over the last three decades. The process presents two challenges to the microorganism;
Butt, Julea N. +5 more
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Multi-heme Cytochromes in Shewanella oneidensis MR-1:Structures, functions and opportunities [PDF]
, 2015 Multi-heme cytochromes are employed by a range of microorganisms to transport electrons over distances of up to tens of nanometers. Perhaps the most spectacular utilization of these proteins is in the reduction of extracellular solid substrates ...
Brown JP +9 more
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The ‘porin-cytochrome’ model for microbe-to-mineral electron transfer [PDF]
, 2012 Many species of bacteria can couple anaerobic growth to the respiratory reduction of insoluble minerals containing Fe(III) or Mn(III/IV). It has been suggested that in Shewanella species electrons cross the outer membrane to extracellular substrates via ‘
Afkar +57 more
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