p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit

Structures of the flavocytochrome p-cresol methylhydroxylase and its enzyme-substrate complex: gated substrate entry and proton relays support the proposed catalytic mechanism

4-cresol dehydrogenase [hydroxylating] flavoprotein subunit

4-cresol dehydrogenase [hydroxylating] cytochrome c subunit

Flavocytochrome c, P-cresol methylhydroxylase cytochrome subunit

PEG 8000, Tris, ammonium acetate, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 296K

Flavocytochrome p-Cresol Methylhydroxylate and its Enzyme-Substrate Complex

4-cresol dehydrogenase [hydroxylating] flavoprotein subunit (E.C.1.17.99.1), 4-cresol dehydrogenase [hydroxylating] cytochrome c subunit (E.C.1.17.99.1)

The biological assembly is a heterotetramer.

FLAVOCYTOCHROME, ELECTRON-TRANSFER, FAD, HEME, OXIDOREDUCTASE