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Characterization of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough

DOI: 10.1016/bs.mie.2018.10.003 DOI Help

Authors: Sonia Zacarias (Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa) , Marisela Vélez (Instituto de Catálisis y Petroleoquímica, CSIC) , Marcos Pita (Instituto de Catálisis y Petroleoquímica, CSIC) , Antonio L. De Lacey (Instituto de Catálisis y Petroleoquímica, CSIC) , Pedro M. Matias (iBET, Instituto de Biologia Experimental e Tecnológica) , Inês A. C. Pereira (Instituto de Tecnologia Química e Biológica António Xavier, Universidade Nova de Lisboa)
Co-authored by industrial partner: No

Type: Book Chapter
ISBN: 0076-6879

State: Published (Approved)
Published: November 2018
Diamond Proposal Number(s): 9378

Abstract: The [NiFeSe] hydrogenases are a subgroup of the well-characterized family of [NiFe] hydrogenases, in which a selenocysteine is a ligand to the nickel atom in the binuclear NiFe active site instead of cysteine. These enzymes display very interesting catalytic properties for biological hydrogen production and bioelectrochemical applications: high H2 production activity, bias for H2 evolution, low H2 inhibition, and some degree of O2 tolerance. Here we describe the methodologies employed to study the [NiFeSe] hydrogenase isolated from the sulfate-reducing bacteria D. vulgaris Hildenborough and the creation of a homologous expression system for production of variant forms of the enzyme.

Journal Keywords: [NiFeSe] hydrogenases; Hydrogen; Selenocysteine; Oxygen tolerance; X-ray crystallography; Desulfovibrio vulgaris Hildenborough; Sulfate-reducing bacteria; Infrared spectroscopy

Subject Areas: Chemistry, Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography