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Biochemistry|March 17, 1992
Reaction of ferrous cytochrome c peroxidase with dioxygen: site-directed mutagenesis provides evidence for rapid reduction of dioxygen by intramolecular electron transfer from the compound I radical siteM A Miller, D Bandyopadhyay, J M Mauro, et al.Biochemical and Biophysical Research Communications|August 31, 1990
Quaternary structure and the geminate recombination of carp hemoglobin with methylisocyanideD Bandyopadhyay, K N Walda, D Magde, et al.The Journal of Biological Chemistry|October 25, 1983
Reactivity of ferrous heme proteins at low pHT G Traylor, L A Deardurff, M Coletta, et al.Biochemistry|October 23, 1990
CO dissociation in cytochrome c peroxidase: site-directed mutagenesis shows that distal Arg 48 influences CO dissociation ratesM A Miller, J M Mauro, G Smulevich, et al.Biochemistry|February 6, 1996
Evidence for a slow tertiary relaxation in the reaction of tert-butyl isocyanide with horseradish peroxidaseD Bandyopadhyay, K N Walda, T M Grogan, et al.The Journal of Biological Chemistry|August 15, 1985
On the structure of heme d1. An isobacteriochlorin derivative as the prosthetic group of dissimilatory nitrite reductase?C K ChangBiochemistry|February 28, 1995
Myoglobin-NO at low pH: free four-coordinated heme in the protein pocketA F Duprat, T G Traylor, G Z Wu, et al.Biochemistry|February 20, 1990
CO recombination in cytochrome c peroxidase: effect of the local heme environment on CO binding explored through site-directed mutagenesisM A Miller, M Coletta, J M Mauro, et al.The Journal of Biological Chemistry|July 5, 1986
The porphinedione structure of heme d1. Synthesis and spectral properties of model compounds of the prosthetic group of dissimilatory nitrite reductaseC K Chang, W WuPageof 17