Literature DB >> 6477480

Direct structural information for the copper site of dopamine beta-mono-oxygenase obtained by using extended X-ray-absorption fine structure.

S S Hasnain, G P Diakun, P F Knowles, N Binsted, C D Garner, N J Blackburn.   

Abstract

Copper K-edge e.x.a.f.s (extended X-ray-absorption fine structure) was measured for dopamine beta-mono-oxygenase in aqueous solution. Comparison with the Cu K-edge e.x.a.f.s. of bovine erythrocyte superoxide dismutase shows a close resemblance. Detailed analysis of the e.x.a.f.s. indicates that the copper atom is bound to four imidazole groups at 0.201 nm with one or two oxygen atoms at 0.23 nm.

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Year:  1984        PMID： 6477480      PMCID： PMC1144072          DOI： 10.1042/bj2210545

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


  7 in total

Review 1.  The state and function of copper in biological systems.

Authors:  R Malkin; B G Malmström
Journal:  Adv Enzymol Relat Areas Mol Biol       Date:  1970

2.  Direct spectrophotometric detection of ascorbate free radical formed by dopamine beta-monooxygenase and by ascorbate oxidase.

Authors:  T Skotland; T Ljones
Journal:  Biochim Biophys Acta       Date:  1980-06-05

3.  Determination and analysis of the 2 A-structure of copper, zinc superoxide dismutase.

Authors:  J A Tainer; E D Getzoff; K M Beem; J S Richardson; D C Richardson
Journal:  J Mol Biol       Date:  1982-09-15       Impact factor: 5.469

4.  An extended X-ray-absorption-fine-structure study of the copper and zinc sites of freeze-dried bovine superoxide dismutase.

Authors:  N J Blackburn; S S Hasnain; G P Diakun; P F Knowles; N Binsted; C D Garner
Journal:  Biochem J       Date:  1983-09-01       Impact factor: 3.857

5.  Dopamine beta-monooxygenase. Binding to apoenzyme and rapid exchange in holoenzyme of 64Cu studied with high-performance size-exclusion gel chromatography.

Authors:  T Skotland; T Flatmark
Journal:  Eur J Biochem       Date:  1983-04-15

6.  An extended-X-ray-absorption-fine-structure study of bovine erythrocyte superoxide dismutase in aqueous solution. Direct evidence for three-co-ordinate Cu(I) in reduced enzyme.

Authors:  N J Blackburn; S S Hasnain; N Binsted; G P Diakun; C D Garner; P F Knowles
Journal:  Biochem J       Date:  1984-05-01       Impact factor: 3.857

7.  Kinetic and e.p.r. studies of cyanide and azide binding to the copper sites of dopamine (3,4-dihydroxyphenethylamine) beta-mono-oxygenase.

Authors:  N J Blackburn; D Collison; J Sutton; F E Mabbs
Journal:  Biochem J       Date:  1984-06-01       Impact factor: 3.857
  7 in total

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