Tomoichirou Kusumoto

ORCID: 0000-0002-8386-831X
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Research Areas
  • Photosynthetic Processes and Mechanisms
  • Microbial Metabolic Engineering and Bioproduction
  • Enzyme Catalysis and Immobilization
  • Enzyme Structure and Function
  • Hemoglobin structure and function
  • Heme Oxygenase-1 and Carbon Monoxide
  • Pharmacological Effects of Natural Compounds
  • Advanced Electron Microscopy Techniques and Applications
  • Amino Acid Enzymes and Metabolism
  • ATP Synthase and ATPases Research
  • Parathyroid Disorders and Treatments
  • Erythrocyte Function and Pathophysiology
  • Renal function and acid-base balance
  • Microbial metabolism and enzyme function
  • Biotin and Related Studies
  • Plant-based Medicinal Research
  • Photoreceptor and optogenetics research
  • Electrochemical sensors and biosensors
  • Electrochemical Analysis and Applications
  • Vitamin K Research Studies
  • Microbial Metabolism and Applications
  • Metabolism and Genetic Disorders
  • Cannabis and Cannabinoid Research

Kyushu Institute of Technology
2011-2025

Kurashiki Central Hospital
1978

Peering into a membrance oxidase Microorganisms have evolved number of enzymes to reduce oxygen and prevent oxidative stress. Cytochrome bd oxidases serve this role also protect pathogenic bacteria from nitric acid; however, class so far has eluded high-resolution crystallography. Safarian et al. were able resolve the three-dimensional structure cytochrome thermophilic bacterium (see Perspective by Cook Poole). The overall triangular arrangement its heme cofactors bear little structural...

10.1126/science.aaf2477 article EN Science 2016-04-28

Mammalian heme oxygenase (HO) catalyzes degradation using reducing equivalents supplied by NADPH-cytochrome P450 reductase (CPR). The tertiary structure of the catalytic domain a constitutively expressed isoform HO, HO-2, resembles that inductive isoform, HO-1, whereas HO-2 has two regulatory motifs (HRM) at proximal portion C-terminus, where disulfide linkage reflects cellular redox conditions and second binding site is located. Here, we report results crosslinking experiments, which...

10.3390/ijms26052318 article EN International Journal of Molecular Sciences 2025-03-05

Cytochromes bd are essential for microaerobic respiration of many prokaryotes including a number human pathogens. These enzymes catalyze the reduction molecular oxygen to water using quinols as electron donors. Their importance prokaryotic survival and absence eukaryotic homologs make these enzyme ideal targets antimicrobial drugs. Here, we determined cryoEM structure menaquinol-oxidizing cytochrome bd-type reductase facultative anaerobic Actinobacterium Corynebacterium glutamicum at...

10.3389/fchem.2022.1085463 article EN cc-by Frontiers in Chemistry 2023-01-04

Corynebacterium glutamicum has a branched respiratory chain: one of the branches is cytochrome bcc complex and aa3-type c oxidase, other bd-type menaquinol oxidase. The factors that influence expression patterns these enzymes remain unclear. To investigate expressional control mechanism enzymes, we have previously constructed promoter assay system utilizing enhanced green fluorescence protein. Here, monitored enzymes' by using this during growth in various culture media, with without Cu(2+)...

10.1080/09168451.2014.968089 article EN Bioscience Biotechnology and Biochemistry 2014-10-23

10.1016/j.bbabio.2012.06.301 article EN publisher-specific-oa Biochimica et Biophysica Acta (BBA) - Bioenergetics 2012-08-09

10.1016/j.bbabio.2016.04.297 article EN publisher-specific-oa Biochimica et Biophysica Acta (BBA) - Bioenergetics 2016-06-04
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