The University of Osaka · 생화학·유전·분자생물학
Genji Kurisu 교수의 연구실은 주로 생물학적 에너지 전환 과정, 특히 광합성 및 산화환원 효소의 구조 기반 기작 해석을 중심으로 연구를 진행하고 있습니다. 특히 시토크롬 b6f 복합체, 복합체 I, [FeFe]-수소효소, 티로신아제 등 다양한 금속 효소의 고해상도 구조를 규명함으로써 전자 이동과 수소 생성 메커니즘을 밝혀내고 있습니다. 이들은 생체 내 에너지 생산과 전환의 핵심 단백질들을 구조적으로 규명함으로써, 천연 효소의 높은 촉매 활성과 기질 특이성을 이해하고, 이를 바탕으로 합성 촉매제 개발에도 기여하고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
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
