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Literature DB >> 4352917

Effect of steady illumination on the binding of carbon monoxide by carboxymethylated cytochrome c.

M T Wilson, M Brunori, J Bonaventura, C Bonaventura.

Abstract

The quantum yield, [unk], is reported for the photodissociation of CO from reduced carboxymethylated cytochrome c. The values of [unk] obtained are low relative to that for myoglobin and are pH-independent, being 0.23 at pH6.1 and 0.27 at pH9.7.

Entities: Chemical Gene

Mesh：

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Year: 1973 PMID： 4352917 PMCID： PMC1177548 DOI： 10.1042/bj1310863

Source DB: PubMed Journal: Biochem J ISSN： 0264-6021 Impact factor: 3.857

5 in total

1. Properties of modified cytochromes. I. Equilibrium and kinetics of the pH-dependent transition in carboxymethylated horse heart cytochrome c.

Authors: M Brunori; M T Wilson; E Antonini
Journal: J Biol Chem Date: 1972-10-10 Impact factor: 5.157

2. Carbon monoxide binding by hemoglobin and myoglobin under photodissociating conditions.

Authors: M Brunori; J Bonaventura; C Bonaventura; E Antonini; J Wyman
Journal: Proc Natl Acad Sci U S A Date: 1972-04 Impact factor: 11.205

3. The effects of alkylation of methionyl residues on the properties of horse cytochrome c.

Authors: A Schejter; I Aviram
Journal: J Biol Chem Date: 1970-04-10 Impact factor: 5.157

4. Production of a "cytochrome c" with myoglobin-like properties by alkylating the cyanide complex with bromoacetate.

Authors: A Schejter; P George
Journal: Nature Date: 1965-06-12 Impact factor: 49.962

5. Studies on the quantum yields of the photodissociation of carbon monoxide from hemoglobin and myoglobin.

Authors: R W Noble; M Brunori; J Wyman; E Antonini
Journal: Biochemistry Date: 1967-04 Impact factor: 3.162

5 in total

4 in total

Effect of steady illumination on the binding of carbon monoxide by carboxymethylated cytochrome c.

1. Properties of modified cytochromes. I. Equilibrium and kinetics of the pH-dependent transition in carboxymethylated horse heart cytochrome c.

2. Carbon monoxide binding by hemoglobin and myoglobin under photodissociating conditions.

3. The effects of alkylation of methionyl residues on the properties of horse cytochrome c.

4. Production of a "cytochrome c" with myoglobin-like properties by alkylating the cyanide complex with bromoacetate.

5. Studies on the quantum yields of the photodissociation of carbon monoxide from hemoglobin and myoglobin.

1. Photochemical electron injection into redox-active proteins.

2. Kinetics of carbon monoxide binding and electron transfer by cytochrome c polymers.

3. The nitrite reductase activity of horse heart carboxymethylated-cytochrome c is modulated by cardiolipin.

4. Heme proteins: quantum yield determined by the pulse method.