Flavohemoglobin: a semisynthetic hydroxylase acting in the absence of reductase
- 1 January 1987
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 109 (2) , 606-607
- https://doi.org/10.1021/ja00236a062
Abstract
No abstract availableThis publication has 7 references indexed in Scilit:
- Reactivity of the amino groups of carbonmonoxyhemoglobin S with glyceraldehyde.Published by Elsevier ,2021
- Monooxygenase activity of human hemoglobin: role of quaternary structure in the preponderant activity of the .beta. subunits within the tetramerBiochemistry, 1984
- SUBSTRATE-SPECIFICITY OF THE MONOOXYGENASE ACTIVITY OF HEMOGLOBIN1984
- The role of hemoglobin in the N-oxidation of 4-chloroanilineBiochimica et Biophysica Acta (BBA) - General Subjects, 1983
- Monooxygenase activities of dioxygenases. Benzphetamine demethylation and aniline hydroxylation reactions catalyzed by indoleamine 2,3-dioxygenase.Journal of Biological Chemistry, 1983
- Studies on the effect of reagent and protein charges on reactivity of the β93 sulfhydryl group of human hemoglobin using selected mutationsArchives of Biochemistry and Biophysics, 1980
- Characterization of Enzyme-like activity of human hemoglobin. Properties of the hemoglobin-P-450 reductase-coupled aniline hydroxylase system.Journal of Biological Chemistry, 1976