Recombinant and In Vitro Expression Systems for Hydrogenases: New Frontiers in Basic and Applied Studies for Biological and Synthesis H2 Production

Christine M. English; Carrie Eckert; Katherine Brown; Michael Seibert; Paul W. King

doi:10.1039/b913426n

Recombinant and In Vitro Expression Systems for Hydrogenases: New Frontiers in Basic and Applied Studies for Biological and Synthesis H2 Production

Christine M. English, Carrie Eckert, Katherine Brown, Michael Seibert, Paul W. King

National Renewable Energy Laboratory

Research output: Contribution to journal › Article › peer-review

43 Scopus Citations

Abstract

This review focuses on recent progress in developing heterologous and recombinant expression as well as in vitro maturation systems for the biosynthesis of active [FeFe] and [NiFe]-hydrogenases, which catalyze the reversible reaction, H₂↔ 2e- + 2H⁺. Activities of [FeFe] and [NiFe]-hydrogenases produced from different recombinant and in vitro maturation approaches are compared. Examples of how hydrogenase expression supports basic and applied studies of these enzymes are presented, and barriers to achieving more viable biological and synthetic H₂-production systems and catalysts are addressed.

Original language	American English
Pages (from-to)	9970-9978
Number of pages	9
Journal	Dalton Transactions
Issue number	45
DOIs	https://doi.org/10.1039/b913426n https://doi.org/10.1039/b913426n
State	Published - 10 Nov 2009

NREL Publication Number

NREL/JA-2A0-46882

Keywords

bioscience
hydrogen

Access to Document

Cite this

@article{0424a02e6afd4e5ebda895186eb030e3,

title = "Recombinant and In Vitro Expression Systems for Hydrogenases: New Frontiers in Basic and Applied Studies for Biological and Synthesis H2 Production",

abstract = "This review focuses on recent progress in developing heterologous and recombinant expression as well as in vitro maturation systems for the biosynthesis of active [FeFe] and [NiFe]-hydrogenases, which catalyze the reversible reaction, H2↔ 2e- + 2H+. Activities of [FeFe] and [NiFe]-hydrogenases produced from different recombinant and in vitro maturation approaches are compared. Examples of how hydrogenase expression supports basic and applied studies of these enzymes are presented, and barriers to achieving more viable biological and synthetic H2-production systems and catalysts are addressed.",

keywords = "bioscience, hydrogen",

author = "English, {Christine M.} and Carrie Eckert and Katherine Brown and Michael Seibert and King, {Paul W.}",

year = "2009",

month = nov,

day = "10",

doi = "10.1039/b913426n",

language = "American English",

pages = "9970--9978",

journal = "Dalton Transactions",

issn = "1477-9226",

publisher = "Royal Society of Chemistry",

number = "45",

}

TY - JOUR

T1 - Recombinant and In Vitro Expression Systems for Hydrogenases: New Frontiers in Basic and Applied Studies for Biological and Synthesis H2 Production

AU - English, Christine M.

AU - Eckert, Carrie

AU - Brown, Katherine

AU - Seibert, Michael

AU - King, Paul W.

PY - 2009/11/10

Y1 - 2009/11/10

N2 - This review focuses on recent progress in developing heterologous and recombinant expression as well as in vitro maturation systems for the biosynthesis of active [FeFe] and [NiFe]-hydrogenases, which catalyze the reversible reaction, H2↔ 2e- + 2H+. Activities of [FeFe] and [NiFe]-hydrogenases produced from different recombinant and in vitro maturation approaches are compared. Examples of how hydrogenase expression supports basic and applied studies of these enzymes are presented, and barriers to achieving more viable biological and synthetic H2-production systems and catalysts are addressed.

AB - This review focuses on recent progress in developing heterologous and recombinant expression as well as in vitro maturation systems for the biosynthesis of active [FeFe] and [NiFe]-hydrogenases, which catalyze the reversible reaction, H2↔ 2e- + 2H+. Activities of [FeFe] and [NiFe]-hydrogenases produced from different recombinant and in vitro maturation approaches are compared. Examples of how hydrogenase expression supports basic and applied studies of these enzymes are presented, and barriers to achieving more viable biological and synthetic H2-production systems and catalysts are addressed.

KW - bioscience

KW - hydrogen

UR - http://www.scopus.com/inward/record.url?scp=72749100414&partnerID=8YFLogxK

U2 - 10.1039/b913426n

DO - 10.1039/b913426n

M3 - Article

C2 - 19904422

AN - SCOPUS:72749100414

SN - 1477-9226

SP - 9970

EP - 9978

JO - Dalton Transactions

JF - Dalton Transactions

IS - 45

ER -

Recombinant and In Vitro Expression Systems for Hydrogenases: New Frontiers in Basic and Applied Studies for Biological and Synthesis H2 Production

Abstract

NREL Publication Number

Keywords

Access to Document

Other files and links

Fingerprint

Cite this