Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus

Antonius C F Gorren, Pierre Moenne-Loccoz, Gabriele Backes, Simon De Vries, Joann Sanders-Loehr, Johannis A. Duine

Research output: Contribution to journalArticle

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Abstract

The nonconvertible substrate analogues di-, tri-, and tetramethylammonium are bound with fairly high affinity to oxidized methylamine dehydrogenase (MADHOX) from Thiobacillus versutus and induce the same red-shift in the optical absorbance spectrum of MADHOX as do the monovalent cations Cs+, Rb+, and NH4 +. Like the monovalent cations, trimethylamine also competitively inhibits the reduction of MADHOX by methylamine. Rapid-scan experiments show that within the first few milliseconds of the reaction between MADHOX and methylamine a red-shifted intermediate is formed as well. Taken together these experiments demonstrate the existence of a common binding site on MADHOX for the substrate CH3NH3 +, the substrate analogues (CH3)2NH2 +, (CH3)3NH+, and (CH3)4N+, and the monovalent cations Cs+, Rb+, and NH4 +. Therefore we conclude that, prior to conversion, methylamine is noncovalently bound to MADHOX as a cation. The resonance Raman spectra of MADHOX in the absence and presence of Cs+, NH4 +, and (CH3)3NH+ are very similar, except for the C=O stretching frequencies oftfie o-quinone carbonyls of the tryptophyltryptophanquinone (TTQ) active center, which show 5-30 cm-1 downshifts. From these Raman results and the X-ray crystal structure, we conclude that the CH3NH3 + binding site is in close proximity to the O6 carbonyl oxygen of the TTQ.

Original languageEnglish (US)
Pages (from-to)12926-12931
Number of pages6
JournalBiochemistry
Volume34
Issue number40
StatePublished - 1995

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Thiobacillus
Monovalent Cations
Binding Sites
Substrates
Stretching
Cations
Raman scattering
Crystal structure
Experiments
X-Rays
Oxygen
X rays
methylamine dehydrogenase
methylamine

ASJC Scopus subject areas

  • Biochemistry

Cite this

Gorren, A. C. F., Moenne-Loccoz, P., Backes, G., De Vries, S., Sanders-Loehr, J., & Duine, J. A. (1995). Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus. Biochemistry, 34(40), 12926-12931.

Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus. / Gorren, Antonius C F; Moenne-Loccoz, Pierre; Backes, Gabriele; De Vries, Simon; Sanders-Loehr, Joann; Duine, Johannis A.

In: Biochemistry, Vol. 34, No. 40, 1995, p. 12926-12931.

Research output: Contribution to journalArticle

Gorren, ACF, Moenne-Loccoz, P, Backes, G, De Vries, S, Sanders-Loehr, J & Duine, JA 1995, 'Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus', Biochemistry, vol. 34, no. 40, pp. 12926-12931.
Gorren ACF, Moenne-Loccoz P, Backes G, De Vries S, Sanders-Loehr J, Duine JA. Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus. Biochemistry. 1995;34(40):12926-12931.
Gorren, Antonius C F ; Moenne-Loccoz, Pierre ; Backes, Gabriele ; De Vries, Simon ; Sanders-Loehr, Joann ; Duine, Johannis A. / Evidence for a methylammonium-binding site on methylamine dehydrogenase of Thiobacillus versutus. In: Biochemistry. 1995 ; Vol. 34, No. 40. pp. 12926-12931.
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