A novel membrane-anchored cytochrome c-550 of alkaliphilic Bacillus clarkii K24-1U: expression, molecular features and properties of redox potential

Extremophiles ◽  
2009 ◽  
Vol 13 (3) ◽  
pp. 491-504 ◽  
Author(s):  
Shinichi Ogami ◽  
Shoichi Hijikata ◽  
Tamotsu Tsukahara ◽  
Yasuhiro Mie ◽  
Toshihide Matsuno ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Redox Potential ◽  
Molecular Features ◽  
Bacillus Clarkii ◽  
Alkaliphilic Bacillus

scholarly journals The effect of complete or specific partial acetimidylation on the biological properties of cytochrome c and cytochrome c-T

1984 ◽  
Vol 217 (3) ◽  
pp. 595-599 ◽  
Author(s):  
C J A Wallace
Keyword(s):  
Structural Change ◽  
Cytochrome C ◽  
Oxygen Uptake ◽  
Redox Potential ◽  
Biological Properties ◽  
Amino Groups ◽  
Cytochromes C ◽  
Restricted Region ◽  
Horse Cytochrome

The biological consequences of acetimidylation of all 19 epsilon-amino groups of horse cytochrome c are a slight decrease in both the redox potential of the protein and its ability to stimulate oxygen uptake in the cytochrome c-depleted-mitochondria assay. Examination of a number of specific partially acetimidylated analogues and acetimidylated cytochromes c of other species has shown that the changes in biological properties, which are associated with a slight structural change as monitored by n.m.r. spectroscopy [Boswell, Moore, Williams, Harris, Wallace, Bocieck & Welti (1983) Biochem. J. 213, 679-686], appear to stem from modification of residues in a restricted region of the sequence. The failure of the redox potential of Saccharomyces cerevisae cytochrome c to be affected by acetimidylation suggests that it is lysine-53, absent from that species, that is the sensitive residue.

Surface Packing Determines the Redox Potential Shift of Cytochrome c Adsorbed on Gold

2014 ◽  
Vol 136 (37) ◽  
pp. 12929-12937 ◽  
Author(s):  
Laura Zanetti-Polzi ◽  
Isabella Daidone ◽  
Carlo Augusto Bortolotti ◽  
Stefano Corni
Keyword(s):  
Cytochrome C ◽  
Redox Potential ◽  
Potential Shift

scholarly journals A new non-covalent complex of semisynthetically modified tryptic fragments of cytochrome c

1986 ◽  
Vol 239 (2) ◽  
pp. 333-337 ◽  
Author(s):  
A E Proudfoot ◽  
C J Wallace ◽  
D E Harris ◽  
R E Offord
Keyword(s):  
Biological Activity ◽  
Cytochrome C ◽  
Redox Potential ◽  
Peptide Bond ◽  
Succinate Oxidation ◽  
Covalent Complex ◽  
Horse Cytochrome

We have prepared a semisynthetic analogue of fully acetimidylated horse cytochrome c, a complex in which the peptide bond between residues glycine-37 and arginine-38 is lacking. In contrast with the complex that we have previously described [Harris & Offord (1977) Biochem. J. 161, 12-25], in which the break in continuity is between residues arginine-38 and lysine-39, the new analogue has a nearly normal redox potential, and can more fully restore succinate oxidation to mitochondria depleted of cytochrome c. Studies of this and other analogues lead us to propose an explanation for the low biological activity of complex (1-38)-(39-104) and a role for the invariance of arginine-38.

scholarly journals The experimental determination of redox-potential of mutated cytochrome c with eight charge changing substitutions

2015 ◽  
Author(s):  
Vasily Ptushenko ◽  
Rita V Chertkova
Keyword(s):  
Cytochrome C ◽  
Redox Potential ◽  
Experimental Determination

The redox potential of the mutated cytochrome c form with eight charge changing substitutions was experimentally determined

Reflectance Spectra and Some Respiratory Reactions of Bovine, Equine and Human Thrombocytes

1957 ◽  
Vol 188 (2) ◽  
pp. 415-419 ◽  
Author(s):  
Charles R. Goucher ◽  
W. Kocholaty
Keyword(s):  
Cytochrome C ◽  
Redox Potential ◽  
Cytochrome Oxidase ◽  
Sodium Azide ◽  
Visible Region ◽  
Reflectance Spectra ◽  
Absorption Bands ◽  
Oxidase System ◽  
Chromatic Properties

Reflectance spectra of human, bovine and equine thrombocytes reveal the existence of pigments which absorb in the visible region of the spectrum. The chromatic properties of these pigments change with the redox potential of the cell. These spectra alterations suggest the existence of a cytochrome system, but the position of the absorption bands does not permit their identification with known mammalian cytochromes. However, platelet homogenates contain a cytochrome oxidase which oxidizes mammalian cytochrome c and which is inhibited by sodium azide. Platelet extracts also contain a DPNH oxidase system which is inhibited by sodium azide.

Characterization of Two Soluble Basic Cytochromes Isolated from the Anoxygenic Phototrophic Sulfur Bacterium Chlorobium phaeobacteroides

1989 ◽  
Vol 44 (1-2) ◽  
pp. 71-76 ◽  
Author(s):  
Ulrich Fischer
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
Redox Potential ◽  
Isoelectric Point ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Chlorobium Phaeobacteroides ◽  
Flavocytochrome C ◽  
Reduced State

Abstract Chlorobium phaeobacteroides contains two soluble basic c-type cytochromes, a flavocytochrome c-552 and a small cytochrome c-555. Both electron transfer proteins were highly purified by ion exchange chromatography and gel filtration. The flavocytochrome c-552 exhibits maxima at 552 nm, 523 nm and 416 nm in the reduced state and at 409.5 nm with two shoulders at 440 nm and 480 nm in the oxidized form. The best purity index (A280/A416)obtained was 0.65. The molecular properties of this flavocytochrome are as follows: isoelectric point, pH 9.5 - 10; redox potential, +63 mV; molecular weight, 56,000. Cytochrome c-555 is a small basic hemoprotein with an isoelectric point of pH 9.5 - 10, a molecular weight of 9,500 and a midpoint redox potential of +105 mV. The best purity index {A280/A418) obtained was 0.176. The oxidized form of this cytochrome has a maximum at 411.5 nm, while the reduced state shows three maxima (α-band at 554.5 nm; β-band at 523 nm, and γ-band at 418 nm). The a-band is asymmetrical with a typical shoulder at 551 nm.

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