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

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

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

scholarly journals Structural implications of the C-terminal tail in the catalytic and stability properties of manganese peroxidases from ligninolytic fungi

2014 ◽  
Vol 70 (12) ◽  
pp. 3253-3265 ◽  
Author(s):  
Elena Fernández-Fueyo ◽  
Sandra Acebes ◽  
Francisco J. Ruiz-Dueñas ◽  
María Jesús Martínez ◽  
Antonio Romero ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Electron Transfer ◽  
Manganese Peroxidase ◽  
Catalytic Properties ◽  
Substrate Oxidation ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Ceriporiopsis Subvermispora ◽  
Ligninolytic Fungi ◽  
Access Channel

The genome ofCeriporiopsis subvermisporaincludes 13 manganese peroxidase (MnP) genes representative of the three subfamilies described in ligninolytic fungi, which share an Mn2+-oxidation site and have varying lengths of the C-terminal tail. Short, long and extralong MnPs were heterologously expressed and biochemically characterized, and the first structure of an extralong MnP was solved. Its C-terminal tail surrounds the haem-propionate access channel, contributing to Mn2+oxidation by the internal propionate, but prevents the oxidation of 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonate) (ABTS), which is only oxidized by short MnPs and by shortened-tail variants from site-directed mutagenesis. The tail, which is anchored by numerous contacts, not only affects the catalytic properties of long/extralong MnPs but is also associated with their high acidic stability. Cd2+binds at the Mn2+-oxidation site and competitively inhibits oxidation of both Mn2+and ABTS. Moreover, mutations blocking the haem-propionate channel prevent substrate oxidation. This agrees with molecular simulations that position ABTS at an electron-transfer distance from the haem propionates of anin silicoshortened-tail form, while it cannot reach this position in the extralong MnP crystal structure. Only small differences exist between the long and the extralong MnPs, which do not justify their classification as two different subfamilies, but they significantly differ from the short MnPs, with the presence/absence of the C-terminal tail extension being implicated in these differences.

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