The University of Osaka · Biochemistry, Genetics and Molecular Biology
Professor Genji Kurisu's research lab specializes in structural biology and bioinorganic chemistry, focusing on the molecular architecture and catalytic mechanisms of metalloenzymes involved in energy conversion and redox metabolism. The lab employs advanced techniques such as X-ray crystallography and cryo-electron microscopy to study complex biological systems, including photosynthetic reaction centers, hydrogenases, cytochrome complexes, and copper-containing enzymes. Their work bridges fundamental enzymology with applications in renewable energy and biocatalysis, particularly in understanding electron transfer, proton pumping, and metal cluster function in biological systems. A central theme is the structural basis of enzyme maturation, activation, and electron transfer in metalloenzymes with medical and biotechnological relevance.
Figures are computed from collected data and may differ slightly.
The cytochrome b6f complex provides the electronic connection between the photosystem I and photosystem II reaction centers of oxygenic photosynthesis and generates a transmembrane electrochemical proton gradient for adenosine triphosphate synthesis. A 3.0 angstrom crystal structure of the dimeric b6f complex from the thermophilic cyanobacterium Mastigocladus laminosus reveals a large quinone exchange cavity, stabilized by lipid, in which plastoquinone, a quinone-analog inhibitor, and a novel he
Plugging into the pump Photosynthetic organisms use light to fix carbon dioxide in a process that requires both chemical reducing equivalents and adenosine triphosphate (ATP). Balancing the ratio of these inputs is accomplished by a short circuit in electron flow through photosynthetic complex I, a proton pump that contributes to ATP production but does not increase net reducing equivalents in the cell. Schuller et al. solved a cryo–electron microscopy structure of photosynthetic complex I (see
[FeFe]-hydrogenases are nature's fastest catalysts for the evolution or oxidation of hydrogen. Numerous synthetic model complexes for the [2Fe] subcluster (2Fe<sub>H</sub>) of their active site are known, but so far none of these could compete with the enzymes. The complex Fe<sub>2</sub>[μ-(SCH<sub>2</sub>)<sub>2</sub>X](CN)<sub>2</sub>(CO)<sub>4</sub><sup>2-</sup> with X = NH was shown to integrate into the apo-form of [FeFe]-hydrogenases to yield a fully active enzyme. Here we report the first
Tyrosinase, a dinuclear copper monooxygenase/oxidase, plays a crucial role in the melanin pigment biosynthesis. The structure and functions of tyrosinase have so far been studied extensively, but the post-translational maturation process from the pro-form to the active form has been less explored. In this study, we provide the crystal structures of Aspergillus oryzae full-length pro-tyrosinase in the holo- and the apo-forms at 1.39 and 2.05 Å resolution, respectively, revealing that Phe(513) on
The structure of the complex of maize sulfite reductase (SiR) and ferredoxin (Fd) has been determined by X-ray crystallography. Co-crystals of the two proteins prepared under different conditions were subjected to the diffraction analysis and three possible structures of the complex were solved. Although topological relationship of SiR and Fd varied in each of the structures, two characteristics common to all structures were found in the pattern of protein-protein interactions and positional arr
A zinc endoprotease produced by Streptomyces caespitosus (ScNP) specifically hydrolyzes the peptide bond at the imino side of aromatic residues and is the smallest protease found to date. Although ScNP carries the zinc-binding sequence HEXXH, its primary structure of 132 amino acid residues differs from those of other known zinc metalloendoproteases. X-ray structural analysis of ScNP at 1.6 Å resolution revealed that despite a lack of sequence homology, the common topological feature of main-cha
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