Results 21 to 30 of about 271,428 (260)

Monooxygenase activity of cytochrome c peroxidase.

Journal of Biological Chemistry, 1992
Recombinant cytochrome c peroxidase (CcP) and a W51A mutant of CcP, in contrast to other classical peroxidases, react with phenylhydrazine to give sigma-bonded phenyl-iron complexes. The conclusion that the heme iron is accessible to substrates is supported by the observation that CcP and W51A CcP oxidize thioanisole to the racemic sulfoxide with ...
V P, Miller, G D, DePillis, J C, Ferrer, A G, Mauk, P R, Ortiz de Montellano   +4 more
openaire   +3 more sources

Respiration triggers heme transfer from cytochrome c peroxidase to catalase in yeast mitochondria. [PDF]

Proc Natl Acad Sci U S A, 2014
Kathiresan M, Martins D, English AM.
europepmc   +2 more sources

Peroxygenase activity of cytochrome c peroxidase and three apolar distal heme pocket mutants: hydroxylation of 1-methoxynaphthalene. [PDF]

BMC Biochem, 2013
Erman JE, Kilheeney H, Bidwai AK, Ayala CE, Vitello LB.   +4 more
europepmc   +3 more sources

Differential Responses in the Core, Active Site and Peripheral Regions of Cytochrome c Peroxidase to Extreme Pressure and Temperature. [PDF]

J Mol Biol
Zawistowski RK, Crane BR.
europepmc   +3 more sources

Studies on Cytochrome c Peroxidase

Journal of Biological Chemistry, 1965
Takashi Yonetani, Gisela S. Ray
  +4 more sources

Pseudomonas Cytochrome c Peroxidase. I. Purification Procedure. [PDF]

Acta Chemica Scandinavica, 1970
Nils Ellfolk, Ritva Soininen, Søren Bols Pedersen, Dagny Holme, Aud Lamvik, Erling Sunde, Nils Andreas Sørensen   +6 more
openaire   +3 more sources

The diheme cytochrome c peroxidase from Shewanella oneidensis requires reductive activation. [PDF]

Biochemistry, 2012
Pulcu GS, Frato KE, Gupta R, Hsu HR, Levine GA, Hendrich MP, Elliott SJ.   +6 more
europepmc   +2 more sources

Naturally Occurring I81N Mutation in Human Cytochrome c Regulates Both Inherent Peroxidase Activity and Interactions with Neuroglobin

ACS Omega, 2022
Human cytochrome c (hCyt c) is a crucial heme protein and plays an indispensable role in energy conversion and intrinsic apoptosis pathways. The sequence and structure of Cyt c were evolutionarily conserved and only a few naturally occurring mutants were
Yuanling Feng, Xichun Liu, Lianzhi Li, Shuqin Gao, G. Wen, Ying Lin   +5 more
semanticscholar   +1 more source

Studies on Cytochrome c Peroxidase

Journal of Biological Chemistry, 1968
T Yonetani, T Asakura
openaire   +2 more sources

Cardiolipin–cytochrome c complex: Switching cytochrome c from an electron‐transfer shuttle to a myoglobin‐ and a peroxidase‐like heme‐protein

IUBMB Life - A Journal of the International Union of Biochemistry and Molecular Biology, 2015
P. Ascenzi, M. Coletta, Michael T. Wilson, L. Fiorucci, M. Marino, F. Polticelli, F. Sinibaldi, R. Santucci   +7 more
semanticscholar   +3 more sources