(Q73169661)

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Conformational dynamics and molecular interaction reactions of recombinant cytochrome p450scc (CYP11A1) detected by fluorescence energy transfer

scientific article published on 01 September 1999

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1 November 2019

Conformational dynamics and molecular interaction reactions of recombinant cytochrome p450scc (CYP11A1) detected by fluorescence energy transfer (English)

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Europe PubMed Central

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1 November 2019

molecular interaction

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G I Lepesheva

1

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1 November 2019

N V Strushkevich

2

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1 November 2019

S A Usanov

3

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1 November 2019

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1 September 1999

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1 November 2019

Biochimica et Biophysica Acta

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1 November 2019

1434

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1 November 2019

1

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1 November 2019

31-43

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1 November 2019

The Energy Landscapes and Motions of Proteins

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Evidence for conformational dynamics and molecular aggregation in cytochrome P450 102 (BM-3)

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The roles of individual amino acids in altering substrate specificity of the P450 2a4/2a5 enzymes

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Carbon monoxide binding to cytochrome P450BM-3: evidence for a substrate-dependent conformational change

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The high-spin/low-spin equilibrium in cytochrome P-450--a new method for determination of the high-spin content.

1 reference

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The cholesterol-side-chain-cleaving cytochrome P450 spin-state equilibrium. 1. Thermodynamic analysis.

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Protein fluorescence, dynamics and function: exploration of analogy between electronically excited and biocatalytic transition states

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Expression of functional bovine cholesterol side chain cleavage cytochrome P450 (P450scc) in Escherichia coli

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Active-site topology of bovine cholesterol side-chain cleavage cytochrome P450 (P450scc) and evidence for interaction of tyrosine 94 with the side chain of cholesterol

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Sensitive assay of cytochrome P450scc activity by high-performance liquid chromatography.

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The domain structure of the cholesterol side-chain cleavage cytochrome P-450 from bovine adrenocortical mitochondria.

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Modification of cytochrome P-450 with fluorescein isothiocyanate.

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Inhibition of electron transfer from adrenodoxin to cytochrome P-450scc by chemical modification with pyridoxal 5'-phosphate: identification of adrenodoxin-binding site of cytochrome P-450scc

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The cholesterol-side-chain-cleaving cytochrome P450 spin-state equilibrium. 2. Conformational analysis

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A mutant T4 lysozyme displays five different crystal conformations

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Conformational change of the heme moiety of the ferrous cytochrome P-450scc-phenyl isocyanide complex upon binding of reduced adrenodoxin

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Identifiers

10.1016/S0167-4838(99)00156-9

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10556557%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10556557%20AND%20SRC:MED&resulttype=core&format=json

1 November 2019

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