Results 221 to 230 of about 279,218 (267)

C-Type cytochromes of Desulfovibrio vulgaris amino acid composition and end groups of cytochrome C553

Biochemical and Biophysical Research Communications, 1970
Abstract Cytochrome c 553 of Desulfovibrio , vulgaris differs in amino acid composition and in molecular weight (9, 100 ± 100) from cytochrome c 3 (12,000) of the same organism. This protein can be easily obtained in crystalline form. It consists of a single polypeptide chain comprising about 80 amino acid residues and bearing a single ...
Mireille Bruschi, Jean Le Gall, Karl Dus
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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
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Classical force field parameters for the heme prosthetic group of cytochrome c

Journal of Computational Chemistry, 2004
AbstractAccurate force fields are essential for describing biological systems in a molecular dynamics simulation. To analyze the docking of the small redox protein cytochrome c (cyt c) requires simulation parameters for the heme in both the reduced and oxidized states. This work presents parameters for the partial charges and geometries for the heme in
Felix, Autenrieth, Emad, Tajkhorshid, Jerome, Baudry, Zaida, Luthey-Schulten   +3 more
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Resonance Raman scattering on the haem group of cytochrome c

Biochemical and Biophysical Research Communications, 1973
Resonance Raman spectra of the haem group of 8 × 10−5 M horse heart ferro- and ferricytochrome c solutions have been obtained. The spectra are almost identical to that of haemoglobin. The frequency of the Raman line near 1370 cm−1, which in haemoglobin is sensitive to the position of the haem iron, indicates that the iron atom of cytochrome c lies in ...
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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
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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, Hiroshi, Nakajima, Takehiro, Ohta, Kalaivani, Ramanathan, Nobuyuki, Takatani, Yoshinori, Naruta, Yoshihito, Watanabe   +6 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.
Hulin, Tai, Toratane, Munegumi, Yasuhiko, Yamamoto   +2 more
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Thermodynamic Data for Myoglobin, Hæmoglobin and Cytochrome-c Reactions, and the Position of the Hæm Groups

Nature, 1955
CONANT1 first put forward the idea that the haems in haemoglobin are held by two bonds of unequal strength between the iron and groups in the protein on both sides of the haem disk, the weaker bond breaking when combination with oxygen, carbon monoxide, etc., occurs.
P, GEORGE, G I, HANANIA
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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 ...
Xiaogang Qu, Tianhong Lu, Shaojun Dong, Chengli Zhou, Therese M. Cotton   +4 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
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