Biological Hydrogen Production: Not so Elementary

Peters et al report their usage of x-ray crystallography to provide the first structural glimpse of the iron-only hydrogenase from the hydrogen-producing, anaerobic bacterium Clostridium pasteurianum.

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Published inScience (American Association for the Advancement of Science) Vol. 282; no. 5395; pp. 1842 - 1843
Main Authors Michael W. W. Adams, Stiefel, Edward I.
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for the Advancement of Science 04.12.1998
American Association for the Advancement of Science
The American Association for the Advancement of Science
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Abstract Peters et al report their usage of x-ray crystallography to provide the first structural glimpse of the iron-only hydrogenase from the hydrogen-producing, anaerobic bacterium Clostridium pasteurianum.
AbstractList Hydrogenase is the family of enzymes that catalyze the interconversion of the smallest molecule, hydrogen gas. Researchers have used x-ray crystallography to determine the structure of iron-only hydrogenase from a hydrogen-producing, anaerobic bacterium. The mechanisms underlying natural hydrogen metabolism and their possible exploitation by catalytic chemists are discussed.
Representatives of most prokaryotic genera, as well as a few eukaryotes, metabolize hydrogen gas and contain hydrogenase. The enzyme was discovered in the 1930s, its requirement for iron was established in the 1950s, and, in the 1980s, many, but not all, hydrogenases were shown to contain nickel as well as iron. Nickel-iron varieties are usually found in microorganisms that consume hydrogen, whereas those that typically produce hydrogen contain iron-only enzymes. The nature of the catalytic sites in hydrogenases has been subject to intense study and conjecture. On page 1853 of this issue, Peters et al. report their use of X-ray crystallography to provide the first structural glimpse of the iron-only hydrogenase from the hydrogen-producing, anaerobic bacterium Clostridium pasteurianum. The resolved array of five iron-sulfur clusters includes the very special "H cluster," which almost certainly is the catalytic site. With an unprecedented nuclearity of six, the H cluster contains two strikingly organometallic iron atoms, with metal-carbon bonds supplied by diatomic ligands, thought to be carbon monoxide (CO) or cyanide (CN super(-)) (or both).
Peters et al report their usage of x-ray crystallography to provide the first structural glimpse of the iron-only hydrogenase from the hydrogen-producing, anaerobic bacterium Clostridium pasteurianum.
Audience Academic
Author Michael W. W. Adams
Stiefel, Edward I.
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Issue 5395
Keywords Molecular structure
Enzyme
Hydrogen
Clostridium pasteurianum
Clostridiales
Review
Metabolism
Hydrogenase
Enzymatic activity
Clostridiaceae
Bacteria
Oxidoreductases
Crystalline structure
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Snippet Hydrogenase is the family of enzymes that catalyze the interconversion of the smallest molecule, hydrogen gas. Researchers have used x-ray crystallography to...
Peters et al report their usage of x-ray crystallography to provide the first structural glimpse of the iron-only hydrogenase from the hydrogen-producing,...
Representatives of most prokaryotic genera, as well as a few eukaryotes, metabolize hydrogen gas and contain hydrogenase. The enzyme was discovered in the...
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SubjectTerms Acetates
Active sites
Analytical, structural and metabolic biochemistry
Animals
Bacteria
Binding Sites
Biochemistry
Biohydrogen
Biological and medical sciences
Carbon Monoxide - chemistry
Chemistry
Clostridium - enzymology
Crystallography
Crystallography, X-Ray
Cyanides - chemistry
Electrons
Enzymes
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Humans
Hydrogen
Hydrogen - metabolism
Hydrogen production
Hydrogenase - chemistry
Hydrogenase - metabolism
Hydrogenation
Iron
Iron - chemistry
Ligands
Molecules
Organic Chemistry
Oxidation-Reduction
Oxidoreductases
Perspectives
Protons
Pyruvic Acid - metabolism
X-rays
Title Biological Hydrogen Production: Not so Elementary
URI https://www.jstor.org/stable/2897006
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