Biological Hydrogen Production: Not So Elementary

  title={Biological Hydrogen Production: Not So Elementary},
  author={Michael W. W. Adams and Edward Ira Stiefel},
  pages={1842 - 1843}
Many organisms metabolize hydrogen gas by means of an enzyme called hydrogenase. The nature of the catalytic sites in the hydrogenases has long been a subject of conjecture and debate. In their Perspective, Adams and Stiefel discuss results reported in the same issue by [ Peters et al .][1] in which x-ray crystallography was used to provide the first structural glimpse of the iron-only hydrogenase from the hydrogen-producing, anaerobic bacterium Clostridium pasteurianum . With this information… 

Role of Fe-hydrogenase in biological hydrogen production

X-ray crystallography and spectroscopic studies reveal that Fe-hydrogenase is a simpler system than the Ni-Fe counterpart, and the role of Fe-Hydrogenase in the microbial production of hydrogen is summarized.

Structural and Functional Features of Formate Hydrogen Lyase, an Enzyme of Mixed-Acid Fermentation from Escherichia coli

Formate hydrogen lyase from Escherichia coli is a membrane-bound complex that oxidizes formic acid to carbon dioxide and molecular hydrogen, which depends on the external pH and the presence of formate.

[FeFe]-hydrogenases and photobiological hydrogen production

Computational simulations of gas diffusion within the Clostridium pasteurianum CpI hydrogenase are reviewed and the protein structure at specific sites along the O2 pathways are modified by site-directed mutagenesis with the goal of generating recombinant enzymes with higher O2 tolerance.

Hydrogenases and hydrogen metabolism in photosynthetic prokaryotes.

The latest findings on transcriptional regulators and the metabolic conditions that regulate the expression of hydrogenases in various photosynthetic prokaryotes are emphasized.

Maturation of the [NiFe] hydrogenases.

Classi¢cation and phylogeny of hydrogenases 1

Comparing the currently available genome sequences suggests that the [NiFe]-H2ase maturation proteins have no similar counterparts in the genomes of organisms possessing [Fe], which would be consistent with the phylogenetic distinctiveness of the two classes of H2ases.

The Functional Complexity of [NiFe] Hydrogenases in Sulfate Reducing Bacteria (Genus; Desulforvibrio spp)

Sulfate-reducing bacteria are categories of bacteria and archaea that can obtain energy by oxidizing organic compounds or molecular hydrogen (H2) while reducing sulfate (SO42−) to hydrogen sulfide

Organometallic iron: the key to biological hydrogen metabolism.





The biological activation of molecular hydrogen to serve as an electron or hydrogen donor is catalyzed by the enzyme hydrogenase, which appears to be the terminal component of the multienzyme systems responsible for photochemical formation of H2 and for evolution of this gas in fermentations of carbohydrates, amino acids, puriies, and related substances.

Biological Formation of Molecular Hydrogen

It is assumed that the original pattern of reactions leading to H2 production has become modified in various ways during the course of biochemical evolution, and this point of view suggests profitable approaches for clarifying a number of problems in the intermediary metabolism of microorganisms which produce or utilize H2.

Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas

The X-ray structure of the heterodimeric Ni–Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been solved at 2.85 Å resolution and suggests plausible electron and proton transfer pathways.

The hydrogen hypothesis for the first eukaryote

A new hypothesis for the origin of eukaryotic cells is proposed, based on the comparative biochemistry of energy metabolism, to have arisen through symbiotic association of an anaerobic, strictly hydrogen-dependent, strictly autotrophic archaebacterium with a eubacterium.

The structure and mechanism of iron-hydrogenases.

  • M. Adams
  • Chemistry
    Biochimica et biophysica acta
  • 1990

Nickel in the catalytically active hydrogenase of Alcaligenes eutrophus

It is concluded that nickel is essential for the catalytic activity of hydrogenase and not involved as a regulatory component in the synthesis of this enzyme.

Structure of the [Nife] Hydrogenase Active Site: Evidence for Biologically Uncommon Fe Ligands

Crystallographic data on the [NiFe] hydrogenase from Desulfovibrio gigas are presented that provide new information on the structure and mode of action of its dihydrogen activating metal center.