Subunit interactions change the heme active-site geometry in p-cresol methylhydroxylase.

Abstract:

:The enzyme p-cresol methylhydroxylase [4-cresol: (acceptor) oxidoreductase (methyl-hydroxylating), EC 1.17.99.1] contains two subunits: a cytochrome c (electron transfer) subunit (cytochrome cpc) and a flavin (catalytic) subunit. When these subunits are separated by isoelectric focusing, a stable cytochrome subunit is obtained. Significant differences are observed between the one-dimensional NMR spectra of oxidized cytochrome cpc and of oxidized p-cresol methylhydroxylase. Analysis of the two-dimensional nuclear Overhauser enhancement and exchange spectroscopy (NOESY) spectrum of reduced cytochrome cpc suggests that the axial ligand, Met-50, of the stable subunit reorients by a rotation about the C gamma-S delta bond when cytochrome cpc binds to the flavin subunit. This reorientation must result in a change in bonding at the heme, which is reflected both in the para-magnetically shifted resonances and in the redox potential. p-Cresol methylhydroxylase thereby provides an interesting example of the coupling of subunit interactions to active-site structure and reactivity.

authors

McLendon GL,Bagby S,Charman JA,Driscoll PC,McIntire WS,Mathews FS,Hill HA

doi

10.1073/pnas.88.21.9463

subject

Has Abstract

pub_date

1991-11-01 00:00:00

pages

9463-7

issue

21

eissn

0027-8424

issn

1091-6490

journal_volume

88

pub_type

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