Electron Transfer from HiPIP to the Photooxidized Tetraheme Cytochrome Subunit ofAllochromatium vinosumReaction Center:  New Insights from Site-Directed Mutagenesis and Computational Studies†

Biochemistry ◽  
2004 ◽  
Vol 43 (2) ◽  
pp. 437-445 ◽  
Author(s):  
Giovanni Venturoli ◽  
Mahir D. Mamedov ◽  
Sheref S. Mansy ◽  
Francesco Musiani ◽  
Massimo Strocchi ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Computational Studies ◽  
Tetraheme Cytochrome

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.

Enhanced Electron Transfer and Lauric Acid Hydroxylation by Site-Directed Mutagenesis of CYP119

2002 ◽  
Vol 124 (20) ◽  
pp. 5684-5691 ◽  
Author(s):  
Laura S. Koo ◽  
Chad E. Immoos ◽  
Michael S. Cohen ◽  
Patrick J. Farmer ◽  
Paul R. Ortiz de Montellano
Keyword(s):  
Electron Transfer ◽  
Lauric Acid ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Acid Hydroxylation

Site-directed mutagenesis reveals that the hydrophobic patch of azurin mediates electron transfer

1990 ◽  
Vol 112 (2) ◽  
pp. 907-908 ◽  
Author(s):  
Mart Van de Kamp ◽  
Rene Floris ◽  
Frits C. Hali ◽  
Gerard W. Canters
Keyword(s):  
Electron Transfer ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Hydrophobic Patch

Importance of the Conserved Lysine 83 Residue ofZea maysCytochromeb561for Ascorbate-Specific Transmembrane Electron Transfer As Revealed by Site-Directed Mutagenesis Studies

Biochemistry ◽  
2009 ◽  
Vol 48 (44) ◽  
pp. 10665-10678 ◽  
Author(s):  
Nobuyuki Nakanishi ◽  
Motiur Md. Rahman ◽  
Yoichi Sakamoto ◽  
Tadakazu Takigami ◽  
Kazuo Kobayashi ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis
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