X-ray structures of recombinant yeast cytochrome c peroxidase and three heme-cleft mutants prepared by site-directed mutagenesis

Biochemistry ◽  
1990 ◽  
Vol 29 (31) ◽  
pp. 7160-7173 ◽  
Author(s):  
Jimin Wang ◽  
J. Matthew Mauro ◽  
Steven L. Edwards ◽  
Stuart J. Oatley ◽  
Laurence A. Fishel ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Recombinant Yeast ◽  
X Ray

Carbon monoxide dissociation in cytochrome c peroxidase: site-directed mutagenesis shows that distal Arg 48 influences carbon monoxide dissociation rates

Biochemistry ◽  
1990 ◽  
Vol 29 (42) ◽  
pp. 9978-9988 ◽  
Author(s):  
Mark A. Miller ◽  
J. Matthew Mauro ◽  
Giulietta Smulevich ◽  
Massimo Coletta ◽  
Joseph Kraut ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis

Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroscopy

Biochemistry ◽  
1988 ◽  
Vol 27 (15) ◽  
pp. 5477-5485 ◽  
Author(s):  
Giulietta Smulevich ◽  
J. Matthew Mauro ◽  
Laurence A. Fishel ◽  
Ann M. English ◽  
Joseph Kraut ◽  
...  
Keyword(s):  
Raman Spectroscopy ◽  
Cytochrome C ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Cytochrome C Peroxidase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Heme Pocket

Site-directed mutagenesis of yeast cytochrome c peroxidase shows histidine 181 is not required for oxidation of ferrocytochrome c

Biochemistry ◽  
1988 ◽  
Vol 27 (26) ◽  
pp. 9081-9088 ◽  
Author(s):  
Mark A. Miller ◽  
James T. Hazzard ◽  
J. Matthew Mauro ◽  
Steven L. Edwards ◽  
Peter C. Simons ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Ferrocytochrome C

Carbon monoxide recombination in cytochrome c peroxidase: effect of the local heme environment on carbon monoxide binding explored through site-directed mutagenesis

Biochemistry ◽  
1990 ◽  
Vol 29 (7) ◽  
pp. 1777-1791 ◽  
Author(s):  
Mark A. Miller ◽  
Massimo Coletta ◽  
J. Matthew Mauro ◽  
Leslie D. Putnam ◽  
Martin F. Farnum ◽  
...  
Keyword(s):  
Carbon Monoxide ◽  
Cytochrome C ◽  
Cytochrome C Peroxidase ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Carbon Monoxide Binding

scholarly journals Structural basis of the stereoselective formation of the spirooxindole ring in the biosynthesis of citrinadins

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Zhiwen Liu ◽  
Fanglong Zhao ◽  
Boyang Zhao ◽  
Jie Yang ◽  
Joseph Ferrara ◽  
...  
Keyword(s):  
High Resolution ◽  
Organic Synthesis ◽  
Indole Alkaloids ◽  
Site Directed Mutagenesis ◽  
Structural Basis ◽  
Directed Mutagenesis ◽  
Computational Studies ◽  
X Ray ◽  
Evolutionary Branch ◽  
Catalytic Mechanisms

AbstractPrenylated indole alkaloids featuring spirooxindole rings possess a 3R or 3S carbon stereocenter, which determines the bioactivities of these compounds. Despite the stereoselective advantages of spirooxindole biosynthesis compared with those of organic synthesis, the biocatalytic mechanism for controlling the 3R or 3S-spirooxindole formation has been elusive. Here, we report an oxygenase/semipinacolase CtdE that specifies the 3S-spirooxindole construction in the biosynthesis of 21R-citrinadin A. High-resolution X-ray crystal structures of CtdE with the substrate and cofactor, together with site-directed mutagenesis and computational studies, illustrate the catalytic mechanisms for the possible β-face epoxidation followed by a regioselective collapse of the epoxide intermediate, which triggers semipinacol rearrangement to form the 3S-spirooxindole. Comparing CtdE with PhqK, which catalyzes the formation of the 3R-spirooxindole, we reveal an evolutionary branch of CtdE in specific 3S spirocyclization. Our study provides deeper insights into the stereoselective catalytic machinery, which is important for the biocatalysis design to synthesize spirooxindole pharmaceuticals.

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