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PMID: 17311415 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

A base-catalyzed mechanism for dark state recovery in the Avena sativa phototropin-1 LOV2 domain.

Biochemistry ·Vol. 46 ·No. 11 ·2007-03-20 ·Pages 3129-37

Alexandre MT, Arents JC, van Grondelle R, Hellingwerf KJ, Kennis JT

Abstract

Phototropins are autophosphorylating serine/threonine kinases responsible for blue-light perception in plants; their action gives rise to phototropism, chloroplast relocation, and opening of stomatal guard cells. The kinase domain constitutes the C-terminal part of Avena sativa phototropin 1. The N-terminal part contains two light, oxygen, or voltage (LOV) sensing domains, LOV1 and LOV2; each binds a flavin mononucleotide (FMN) chromophore (lambdamax = 447 nm, termed D447) and forms the light-sensitive domains, of which LOV2 is the principal component. Blue-light absorption produces a covalent adduct between a very conserved nearby cysteine residue and the C(4a) atom of the FMN moiety via the triplet state of the flavin. The covalent adduct thermally decays to regenerate the D447 dark state, with a rate that may vary by several orders of magnitude between different species. We report that the imidazole base can act as a very efficient enhancer of the dark recovery of A. sativa phot1 LOV2 (AsLOV2) and some other well-characterized LOV domains. Imidazole accelerates the thermal decay of AsLOV2 by 3 orders of magnitude in the submolar concentration range, via a base-catalyzed mechanism involving base abstraction of the FMN N(5)-H adduct state and subsequent reprotonation of the reactive cysteine. The LOV2 crystal structure suggests that the imidazole molecules may act from a cavity located in the vicinity of the FMN, explaining its high efficiency, populated through a channel connecting the cavity to the protein surface. Use of pH titration and chemical inactivation by diethyl pyrocarbonate (DEPC) suggests that histidines located at the surface of the LOV domain act as base catalysts via an as yet unidentified H-bond network, operating at a rate of (55 s)-1 at pH 8. In addition, molecular processes other than histidine-mediated base catalysis contibute significantly to the total thermal decay rate of the adduct and operate at a rate constant of (65 s)-1, leading to a net adduct decay time constant of 30 s at pH 8.

MeSH Terms
Amino Acid Sequence Avena/metabolism Darkness Diethyl Pyrocarbonate/chemistry Flavin Mononucleotide/chemistry Flavoproteins/chemistry,physiology Histidine/chemistry Hydrogen-Ion Concentration Imidazoles/chemistry Kinetics Models, Molecular Phototropism Protein Serine-Threonine Kinases/chemistry,physiology Protein Structure, Tertiary
Chemicals
Flavoproteins Imidazoles Histidine Flavin Mononucleotide Protein Serine-Threonine Kinases Diethyl Pyrocarbonate
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Alexandre Maxime T A
Department of Biophysics, Faculty of Sciences, Vrije Universiteit, De Boelelaan 1081, 1081HV Amsterdam, The Netherlands. [email protected]
Arents Jos C
van Grondelle Rienk
Hellingwerf Klaas J
Kennis John T M
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
2007-03-20
Epub
2007-00-21
Pages
3129-37
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Grants
NCRR NIH HHS · P41 RR-01081 · United States
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