scholarly journals Correction: One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath)

2019 ◽  
Vol 10 (36) ◽  
pp. 8490-8490
Author(s):  
Hannah R. Adams ◽  
Callie Krewson ◽  
Jenny E. Vardanega ◽  
Sotaro Fujii ◽  
Tadeo Moreno-Chicano ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Methylococcus Capsulatus

Correction for ‘One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath)’ by Hannah R. Adams et al., Chem. Sci., 2019, 10, 3031–3041.

scholarly journals Cytochrome c' of Methylococcus Capsulatus Bath

1996 ◽  
Vol 240 (3) ◽  
pp. 684-691 ◽  
Author(s):  
James A. Zahn ◽  
David M. Arciero ◽  
Alan B. Hooper ◽  
Alan A. Dispirito
Keyword(s):  
Cytochrome C ◽  
Methylococcus Capsulatus

Cytochrome c peroxidase from Methylococcus capsulatus Bath

1997 ◽  
Vol 168 (5) ◽  
pp. 362-372 ◽  
Author(s):  
James A. Zahn ◽  
David M. Arciero ◽  
A. B. Hooper ◽  
Joel R. Coats ◽  
A. A. DiSpirito
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Methylococcus Capsulatus

scholarly journals Correction: One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath)

2019 ◽  
Vol 10 (10) ◽  
pp. 3143-3143
Author(s):  
Hannah R. Adams ◽  
Callie Krewson ◽  
Jenny E. Vardanega ◽  
Sotaro Fujii ◽  
Tadeo Moreno-Chicano ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Methylococcus Capsulatus

Correction for ‘One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath)’ by Hannah R. Adams et al., Chem. Sci., 2019, DOI: 10.1039/c8sc05210g.

scholarly journals One fold, two functions: cytochrome P460 and cytochrome c′-β from the methanotroph Methylococcus capsulatus (Bath)

2019 ◽  
Vol 10 (10) ◽  
pp. 3031-3041 ◽  
Author(s):  
Hannah R. Adams ◽  
Callie Krewson ◽  
Jenny E. Vardanega ◽  
Sotaro Fujii ◽  
Tadeo Moreno ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Methylococcus Capsulatus ◽  
Protein Folds ◽  
Similar Protein ◽  
Spectroscopic Characterisation

Structural and spectroscopic characterisation of cytochrome c′-β and cytochrome P460 from M. capsulatus (Bath) reveals highly similar protein folds but very different heme pockets, providing functional insights.

scholarly journals The amino acid sequence of cytochrome c-555 from the methane-oxidizing bacterium Methylococcus capsulatus

1986 ◽  
Vol 233 (2) ◽  
pp. 333-337 ◽  
Author(s):  
R P Ambler ◽  
H Dalton ◽  
T E Meyer ◽  
R G Bartsch ◽  
M D Kamen
Keyword(s):  
Amino Acid ◽  
Cytochrome C ◽  
Amino Acid Sequence ◽  
Polypeptide Chain ◽  
Cysteine Residues ◽  
British Library ◽  
Methylococcus Capsulatus ◽  
Methionine Residue ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

The amino acid sequence of the cytochrome c-555 from the obligate methanotroph Methylococcus capsulatus strain Bath (N.C.I.B. 11132) was determined. It is a single polypeptide chain of 96 residues, binding a haem group through the cysteine residues at positions 19 and 22, and the only methionine residue is a position 59. The sequence does not closely resemble that of any other cytochrome c that has yet been characterized. Detailed evidence for the amino acid sequence of the protein has been deposited as Supplementary Publication SUP 50131 (12 pages) at the British Library Lending Division, Boston Spa, West Yorkshire LS23 7BQ, U.K., from whom copies are available on prepayment.

scholarly journals Identification of a copper-repressible C-type heme protein of Methylococcus capsulatus (Bath). A member of a novel group of the bacterial di-heme cytochrome c peroxidase family of proteins

FEBS Journal ◽  
2005 ◽  
Vol 272 (24) ◽  
pp. 6324-6335 ◽  
Author(s):  
Odd A. Karlsen ◽  
Louise Kindingstad ◽  
Solveig M. Angelskar ◽  
Live J. Bruseth ◽  
Daniel Straume ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Heme Protein ◽  
Methylococcus Capsulatus

Nucleic Acid Molecules Prepared by Monolayer Techniques

1972 ◽  
Vol 30 ◽  
pp. 178-179
Author(s):  
Dimitrij Lang
Keyword(s):  
Electron Microscopy ◽  
Standard Deviation ◽  
Nucleic Acid ◽  
Cytochrome C ◽  
Nucleic Acids ◽  
Contour Length ◽  
Sample Standard Deviation ◽  
Molecular Weights ◽  
Length Measurements ◽  
Protein Monolayer

The success of the protein monolayer technique for electron microscopy of individual DNA molecules is based on the prevention of aggregation and orientation of the molecules during drying on specimen grids. DNA adsorbs first to a surface-denatured, insoluble cytochrome c monolayer which is then transferred to grids, without major distortion, by touching. Fig. 1 shows three basic procedures which, modified or not, permit the study of various important properties of nucleic acids, either in concert with other methods or exclusively:1) Molecular weights relative to DNA standards as well as number distributions of molecular weights can be obtained from contour length measurements with a sample standard deviation between 1 and 4%.

Activation of cytochrome c to a peroxidase compound I-type intermediate by H2O2: relevance to redox signalling in apoptosis

2004 ◽  
Vol 71 ◽  
pp. 97-106 ◽  
Author(s):  
Mark Burkitt ◽  
Clare Jones ◽  
Andrew Lawrence ◽  
Peter Wardman
Keyword(s):  
Cytochrome C ◽  
Hydroxyl Radical ◽  
Redox Regulation ◽  
Chemotherapeutic Agents ◽  
Tyrosyl Radical ◽  
Compound I ◽  
Definitive Evidence ◽  
Enhanced Production ◽  
Physico Chemical

The release of cytochrome c from mitochondria during apoptosis results in the enhanced production of superoxide radicals, which are converted to H2O2 by Mn-superoxide dismutase. We have been concerned with the role of cytochrome c/H2O2 in the induction of oxidative stress during apoptosis. Our initial studies showed that cytochrome c is a potent catalyst of 2′,7′-dichlorofluorescin oxidation, thereby explaining the increased rate of production of the fluorophore 2′,7′-dichlorofluorescein in apoptotic cells. Although it has been speculated that the oxidizing species may be a ferryl-haem intermediate, no definitive evidence for the formation of such a species has been reported. Alternatively, it is possible that the hydroxyl radical may be generated, as seen in the reaction of certain iron chelates with H2O2. By examining the effects of radical scavengers on 2′,7′-dichlorofluorescin oxidation by cytochrome c/H2O2, together with complementary EPR studies, we have demonstrated that the hydroxyl radical is not generated. Our findings point, instead, to the formation of a peroxidase compound I species, with one oxidizing equivalent present as an oxo-ferryl haem intermediate and the other as the tyrosyl radical identified by Barr and colleagues [Barr, Gunther, Deterding, Tomer and Mason (1996) J. Biol. Chem. 271, 15498-15503]. Studies with spin traps indicated that the oxo-ferryl haem is the active oxidant. These findings provide a physico-chemical basis for the redox changes that occur during apoptosis. Excessive changes (possibly catalysed by cytochrome c) may have implications for the redox regulation of cell death, including the sensitivity of tumour cells to chemotherapeutic agents.

Solution structure of cytochrome b5 mutant (E44/48/56A/D60A) and its interaction with cytochrome c

2001 ◽  
Vol 268 (6) ◽  
pp. 1620-1630
Author(s):  
Yibing Wu ◽  
Yunhua Wang ◽  
Chengmin Qian ◽  
Jun Lu ◽  
Ercheng Li ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Solution Structure ◽  
Cytochrome B5
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