Results 311 to 320 of about 2,436,389 (378)

Promiscuity of heme groups in the cyanobacterial cytochrome-C oxidase.

Biochemistry and molecular biology international, 1996
The cyanobacteria Nostoc sp. strain Mac, Anabaena 7937, Synechocystis 6803, and Anacystis nidulans (Synechococcus 6301) were grown and incubated in the light under three different oxygen regimes: Phase-A cells were harvested from photoautotrophically growing cultures at a cell density of 2.8-3.2 microliter packed cell mass/ml and an oxygen ...
G, Auer, B, Mayer, M, Wastyn, S, Fromwald, K, Eghbalzad, D, Alge, G A, Peschek   +6 more
openaire   +2 more sources

The Effect of Nalidixic Acid Group Compounds on Reduction of Cytochrome c from Horse Heart and Candida krusei [PDF]

Journal of General Microbiology, 1978
Reduction of cytochrome c from both horse heart and Candida krusei by FeSO4 has been demonstrated. This reaction was stimulated by nalidixic acid and structurally related compounds, and the effect was more pronounced for the yeast cytochrome. Divalent metal ions other than Fe2+ lessened or abolished the stimulation by these compounds.
Shigeru Yamabe
openalex   +3 more sources

Schizophrenia Induces Oxidative Stress and Cytochrome C Release in Isolated Rat Brain Mitochondria: a Possible Pathway for Induction of Apoptosis and Neurodegeneration

Iranian journal of pharmaceutical research, 2014
Schizophrenia is a chronic and often debilitating illness which affects about 1% of the world population. Some reagents have been used to simulate schizophrenic disorders in laboratory animals, such as amphetamine and ketamine.
M. Faizi, A. Salimi, Motahareh Rasoulzadeh, P. Naserzadeh, J. Pourahmad   +4 more
semanticscholar   +1 more source

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.
Hulin Tai, Toratane Munegumi, Yasuhiko Yamamoto   +2 more
openalex   +3 more sources

Modification of Functional Group on the CytochromecUsing SPDP Method

Molecular Crystals and Liquid Crystals Science and Technology. Section A. Molecular Crystals and Liquid Crystals, 2001
Abstract To make a molecular assembly of cytochrome c onto the Au substrate, the cytochrome c was modified using the 2-succinimidyl-3-(2-pyridyldi-th-io)propionate(SPDP), so the functional group on the cytochrome c surface was modified. And the modified cytochrome c was adsorbed onto the Au substrate.
Jeong-Woo Choi, Sei-Jeong Park, Byung-Keun Oh, Won Hong Lee, Masamichi Fujihira   +4 more
openaire   +1 more source

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, Hiroshi, Nakajima, Takehiro, Ohta, Kalaivani, Ramanathan, Nobuyuki, Takatani, Yoshinori, Naruta, Yoshihito, Watanabe   +6 more
openaire   +2 more sources

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 ...
Xiaogang Qu, Tianhong Lu, Shaojun Dong, Chengli Zhou, Therese M. Cotton   +4 more
openaire   +1 more source

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.
Hans Senn, Michael A. Cusanovich, Kurt Wüthrich   +2 more
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The multiplicity and stoichiometry of the prosthetic groups in QH2 : Cytochrome c oxidoreductase as studied by EPR

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1979
1. The EPR signal in the g = 2 region of the reduced QH2: cytochrome c oxidoreductase as present in submitochondrial particles and the isolated enzyme is an overlap of two signals in a 1 : 1 weighted ratio. Both signals are due to [2Fe-2S]+1 centers. 2.
S, de Vries, S P, Albracht, F J, Leeuwerik   +2 more
openaire   +2 more sources

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.
F E, Verheul, J W, Draijer, A O, Muijsers, B F, Van Gelder   +3 more
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