Enzymatic and Electron Transfer Activities in Crystalline Protein Complexes (∗)

Enzymatic and electron transfer activities have been studied by polarized absorption spectroscopy in single crystals of both binary and ternary complexes of methylamine dehydrogenase (MADH) with its redox partners. Within the crystals, MADH oxidizes methylamine, and the electrons are passed from the...

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Bibliographic Details
Published in:The Journal of biological chemistry 1996-04, Vol.271 (16), p.9177-9180
Main Authors: Merli, Angelo, Brodersen, Ditlev E., Morini, Barbara, Chen, Zhi-wei, Durley, Rosemary C.E., Mathews, F. Scott, Davidson, Victor L., Rossi, Gian Luigi
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Binding Sites
Copper
Crystallization
Cytochrome c Group - chemistry
Cytochrome c Group - metabolism
Electron Transport
Heme
Indolequinones
Macromolecular Substances
Models, Structural
Oxidoreductases Acting on CH-NH Group Donors - chemistry
Oxidoreductases Acting on CH-NH Group Donors - metabolism
Protein Structure, Secondary
Quinones - metabolism
Spectrophotometry - methods
Tryptophan - analogs & derivatives
Tryptophan - metabolism
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Summary:Enzymatic and electron transfer activities have been studied by polarized absorption spectroscopy in single crystals of both binary and ternary complexes of methylamine dehydrogenase (MADH) with its redox partners. Within the crystals, MADH oxidizes methylamine, and the electrons are passed from the reduced tryptophan tryptophylquinone (TTQ) cofactor to the copper of amicyanin and to the heme of cytochrome c551i via amicyanin. The equilibrium distribution of electrons among the cofactors, and the rate of heme reduction after reaction with substrate, are both dependent on pH. The presence of copper in the ternary complex is not absolutely required for electron transfer from TTQ to heme, but its presence greatly enhances the rate of electron flow to the heme.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.271.16.9177