Results 251 to 260 of about 267,841 (294)

Spectroscopic Properties of a Mitochondrial Cytochromecwith a Single Thioether Bond to the Heme Prosthetic Group

Biochemistry, 2002
The yeast iso-1-cytochrome c variant Cys14Ser has been prepared in which one of the two thioether bonds by which the heme prosthetic group is normally bound to the protein has been eliminated. Comparison of the properties of this variant with those of the wild-type cytochrome provides insight into the role of this covalent attachment of the heme group ...
A. Grant Mauk, Federico I. Rosell
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Internal Electron Transfer in Cytochrome c Oxidase Is Coupled to the Protonation of a Group Close to the Bimetallic Site

Biochemistry, 1994
Absorbance changes following CO dissociation by flash photolysis from mixed-valence cytochrome oxidase have been followed in the Soret and alpha regions. Apart from CO dissociation and recombination, three kinetic phases with rate constants in the range 10(5)-10(3) s-1 at pH 7.5 can be resolved in both spectral regions. The slowest one of these phases,
Peter Brzezinski, Bo G. Malmström, Stefan Hallen   +2 more
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Stability of the Heme Fe−N-Terminal Amino Group Coordination Bond in Denatured Cytochrome c

Inorganic Chemistry, 2008
In the denatured states of Hydrogenobacter thermophilus cytochrome c(552) (HT) and Pseudomonas aeruginosa cytochrome c(551) (PA), and their mutants, the N-terminal amino group of the polypeptide chain is coordinated to heme Fe in place of the axial Met, the His-N(term) form being formed.
Toratane Munegumi, Yasuhiko Yamamoto, Hulin Tai   +2 more
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Electrochemical reaction of cytochrome c at gold electrodes modified with thiophene containing one functional group

Bioelectrochemistry and Bioenergetics, 1994
Abstract The electrochemical reactions of cytochrome c were studied at a thiophene-modified gold electrode. It was demonstrated that thiophene is an effective promoter, although there is only one functional group in the molecule. Based on this result, the mechanism for accelerating the electron transfer process between cytochrome c and the ...
Chengli Zhou, Shaojun Dong, Xiaogang Qu, Therese M. Cotton, Tianhong Lu   +4 more
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1H-NMR assignments for the heme group and electronic structure in Chlorobium thiosulfatophilum cytochrome c-555

Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984
Abstract Cytochrome c-555 from Chlorobium thiosulfatophilum was investigated by 1H nuclear magnetic resonance at 360 MHz. Individual 1H-NMR assignments were obtained for heme c, and the side-chain proton resonances of the axial methionine and the imidazole ring proton lines of the axial histidine were identified.
Michael A. Cusanovich, Hans Martin Senn, Kurt Wüthrich   +2 more
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REACTIVITY OF THIOL GROUPS IN CYTOCHROME c OXIDASE [PDF]

Biochemical Society Transactions, 1981
J. W. Draijer, Frans E.A.M. Verheul, I. K. Dentener, Anton O. Muijsers   +3 more
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Possible Mechanism of Proton Transfer through Peptide Groups in the H-Pathway of the Bovine Cytochrome c Oxidase

Journal of the American Chemical Society, 2007
The peptide group connecting Tyr440 and Ser441 of the bovine cytochrome c oxidase is involved in a recently proposed proton-transfer path (H-path) where, at variance with other pathways (D- and K-paths), a usual hydrogen-bond network is interrupted, thus making this proton propagation rather unconventional.
Atsushi Oshiyama, Mauro Boero, Kenji Shiraishi, Masaru Tateno, Katsumasa Kamiya   +4 more
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The reactivity of thiol groups in bovine heart cytochrome c oxidase towards 5,5′-dithiobis(2-nitrobenzoic acid)

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1982
Bovine heart cytochrome c oxidase consists of 12 stoicheiometric polypeptide chains of at least 11 different types. The enzyme contains 14--16 cysteine residues; the distribution of nearly all cysteine residues over the subunits has been established.
Frans E.A.M. Verheul, Bob F. Van Gelder, J. Wim Draijer, Anton O. Muijsers   +3 more
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Graphene oxide derivatives with variable alkyl chain length and terminal functional groups as supports for stabilization of cytochrome c

International Journal of Biological Macromolecules, 2016
In this study we report the ability of reduced and non-reduced graphene oxide-based nanomaterials (GONs), modified with variable alkyl chain length and terminal functional groups, to act as effective scaffolds for the immobilization of cytochrome c (cyt c) using different immobilization procedures.
Dimitrios Gournis, Michaela Patila, Antonios Kouloumpis, Konstantinos Spyrou, Haralambos Stamatis, Konstantinos Dimos, Ioannis V. Pavlidis, Petros Katapodis   +7 more
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Cytochrome c₅₅₂ from Thermus thermophilus Engineered for Facile Substitution of Prosthetic Group

Biochemistry, 2011
The facile replacement of heme c in cytochromes c with non-natural prosthetic groups has been difficult to achieve due to two thioether linkages between cysteine residues and the heme. Fee et al. demonstrated that cytochrome c(552) from Thermus thermophilus, overproduced in the cytosol of E.
Sk. Md. Ibrahim, Nobuyuki Takatani, Kalaivani Ramanathan, Takehiro Ohta, Yoshihito Watanabe, Hiroshi Nakajima, Yoshinori Naruta   +6 more
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