about
Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5.Engineered and Native Coenzyme B12-dependent Isovaleryl-CoA/Pivalyl-CoA Mutase.Heme-based globin-coupled oxygen sensors: linking oxygen binding to functional regulation of diguanylate cyclase, histidine kinase, and methyl-accepting chemotaxisCofactor Editing by the G-protein Metallochaperone Domain Regulates the Radical B12 Enzyme IcmF.Heme-binding characteristics of the isolated PAS-A domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms.Heme-binding characteristics of the isolated PAS-B domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms.Important roles of Tyr43 at the putative heme distal side in the oxygen recognition and stability of the Fe(II)-O2 complex of YddV, a globin-coupled heme-based oxygen sensor diguanylate cyclase.Pressure effects reveal that changes in the redox states of the heme iron complexes in the sensor domains of two heme-based oxygen sensor proteins, EcDOS and YddV, have profound effects on their flexibility.Introduction of water into the heme distal side by Leu65 mutations of an oxygen sensor, YddV, generates verdoheme and carbon monoxide, exerting the heme oxygenase reaction.Probing the ligand recognition and discrimination environment of the globin-coupled oxygen sensor protein YddV by FTIR and time-resolved step-scan FTIR spectroscopy.Leu65 in the heme distal side is critical for the stability of the Fe(II)-O2 complex of YddV, a globin-coupled oxygen sensor diguanylate cyclase.Kinetic Analysis of a Globin-Coupled Histidine Kinase, AfGcHK: Effects of the Heme Iron Complex, Response Regulator, and Metal Cations on Autophosphorylation Activity.Identification and Characterization of a Redox Sensor Phosphodiesterase from Ferrovum sp. PN-J185 Containing Bacterial Hemerythrin and HD-GYP DomainsStructure determination of the human TRPV1 ankyrin-repeat domain under nonreducing conditionsOptimal Mutant Model of Human S100A3 Protein Citrullinated at Arg51 by Peptidylarginine Deiminase Type III and Its Solution Structural Properties
P50
Q35371781-0580C128-1900-4C71-9D92-3964FE39015CQ35953185-281B58D3-8529-42C2-BD42-A0CAC4829745Q37201164-76907333-92C1-493C-9EF2-038CBA3EB46DQ37705601-0A7BE1AC-76E6-4967-8ABF-902BA5AE0F0BQ38291000-867345A9-3EE6-481A-95CD-34D311A54E89Q38340404-FC4926AB-D2E6-469A-80BE-A864F041376EQ42823317-5FC86EAF-0581-4EC3-99C3-3A62F5E21B56Q44566730-1D867148-8BD3-4B27-9045-49BAE4EAA5E3Q46863741-44CFB037-AAC9-48C1-B907-EA6B57A04A91Q53471184-6C7A6343-F21B-43D4-A926-69BD8D608D29Q54350630-5301C66C-98DE-47C2-9C43-1A0A1D5F82E2Q55052351-A455E722-5486-4928-B64A-EA13787CF6D6Q89654562-A7790658-3630-4137-9F30-88F6B40561F1Q90060448-47AB62BF-738F-4F47-85F7-EC28FDF7E834Q90153437-A473DC17-9BB0-475C-9B3A-DED8F2818A2B
P50
description
investigador
@es
researcher
@en
wetenschapper
@nl
name
Kenichi Kitanishi
@en
Kenichi Kitanishi
@nl
type
label
Kenichi Kitanishi
@en
Kenichi Kitanishi
@nl
prefLabel
Kenichi Kitanishi
@en
Kenichi Kitanishi
@nl
P31
P496
0000-0002-2110-8104