Results 241 to 250 of about 267,841 (294)
Reactive Amino Groups in Baker's Yeast Cytochrome c
The Journal of Biochemistry, 1966 Chiaki Sato, Koiti Titani, Kozo Narita
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The Spectrophotometric Titration of the Phenolic Groups of Horse Heart Cytochrome c*
Biochemistry, 1964 Earle Stellwagen
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A reversible reaction between the ϵ-amino groups of cytochrome C and salicylaldehyde
Biochemical and Biophysical Research Communications, 1966 J.N. Williams, Ruth Jacobs
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Surface of Cytochromec: Infrared Spectroscopy of Carboxyl Groups
Biochemistry, 1997The carboxylate groups of organic acids give strong absorption in the infrared between approximately 1550 and 1650 cm-1. For acetate and chloroacetate derivatives, the infrared (IR) frequency of the carboxylate antisymmetric stretching mode (v(a)OCO) is related to the square root of the pK of the acid, with a shift of approximately 20 cm-1 to higher ...
Jane M. Vanderkooi +2 more
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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 ...
Karl Dus, Mireille Bruschi, Jean Le Gall
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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 ...
Karl Dus, Mireille Bruschi, Jean Le Gall
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Classical force field parameters for the heme prosthetic group of cytochrome c
Journal of Computational Chemistry, 2004AbstractAccurate 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
Zaida Luthey-Schulten +3 more
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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.
Simon de Vries +2 more
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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.
Simon de Vries +2 more
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Resonance Raman scattering on the haem group of cytochrome c
Biochemical and Biophysical Research Communications, 1973Resonance 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, 2001Abstract 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.
Won Hong Lee +4 more
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The pH dependence of the stereochemistry around the heme group in NO–cytochrome c (horse heart)
Inorganica Chimica Acta, 1988The electronic absorption, EPR and MCD spectra of NO derivatives of both ferrous and ferric cytochrome c (horse heart) have been measured in the pH region 2.0 to 12.9, in order to elucidate the pH dependence of the stereochemistry around the heme group.
Tetsushiko Yoshimura, Shinnichiro Suzuki
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