Interplay of acidic residues in the proton channel of E. coli cytochrome bd-I oxidase to promote oxygen reduction and NO releaseBIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICSIF2.72025-04-011OAAI
Function of Escherichia coli bd-I and bd-II oxidaseBIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICSIF2.72024-09-010PRE
Exploring ND-011992, a quinazoline-type inhibitor targeting quinone reductases and quinol oxidasesSCIENTIFIC REPORTSIF3.92023-07-282OAAI
Mutating the environment of heme b595 of E. coli cytochrome bd-I oxidase shifts its redox potential by 200 mV without inactivating the enzymeBIOELECTROCHEMISTRYIF4.52023-06-011OAAI
pH-dependent kinetics of NO release from E. coli bd-I and bd-II oxidase reveals involvement of Asp/Glu58BBIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICSIF2.72023-04-015OAAI
E. coli cytochrome bd-I requires Asp58 in the CydB subunit for catalytic activityFEBS LETTERSIF32022-09-044PRE
Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin DBIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICSIF2.72022-09-010OAAI
Structure of Escherichia coli cytochrome bd-II type oxidase with bound aurachin DNATURE COMMUNICATIONSIF15.72021-11-1132OAAI
Homologous bd oxidases share the same architecture but differ in mechanismNATURE COMMUNICATIONSIF15.72019-11-1374OAAI
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