Protein Side-Chain Motion and Hydration in Proton-Transfer Pathways. Results for Cytochrome P450cam

2003 ◽  
Vol 125 (13) ◽  
pp. 3931-3940 ◽  
Author(s):  
Srabani Taraphder ◽  
Gerhard Hummer
Keyword(s):  
Proton Transfer ◽  
Side Chain ◽  
Cytochrome P450cam ◽  
Side Chain Motion

scholarly journals Corrigendum: Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion

2012 ◽  
Vol 51 (40) ◽  
pp. 9959-9959
Author(s):  
Paul Schanda ◽  
Matthias Huber ◽  
Jérôme Boisbouvier ◽  
Beat H. Meier ◽  
Matthias Ernst
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Dipolar Couplings ◽  
Side Chain ◽  
Side Chain Motion ◽  
Insight Into

Solid-State NMR Measurements of Asymmetric Dipolar Couplings Provide Insight into Protein Side-Chain Motion

2011 ◽  
Vol 50 (46) ◽  
pp. 11005-11009 ◽  
Author(s):  
Paul Schanda ◽  
Matthias Huber ◽  
Jérôme Boisbouvier ◽  
Beat H. Meier ◽  
Matthias Ernst
Keyword(s):  
Solid State ◽  
Solid State Nmr ◽  
Dipolar Couplings ◽  
Side Chain ◽  
Side Chain Motion ◽  
Insight Into

scholarly journals Intracellular Proton-Transfer Mutants in a CLC Cl−/H+ Exchanger

2009 ◽  
Vol 133 (2) ◽  
pp. 131-138 ◽  
Author(s):  
Hyun-Ho Lim ◽  
Christopher Miller
Keyword(s):  
Proton Transfer ◽  
Mutational Analysis ◽  
Side Chain ◽  
Side Chains ◽  
Extracellular Water ◽  
Wild Type ◽  
Cl Transport ◽  
Structural And Functional Properties ◽  
Key Residues

CLC-ec1, a bacterial homologue of the CLC family’s transporter subclass, catalyzes transmembrane exchange of Cl− and H+. Mutational analysis based on the known structure reveals several key residues required for coupling H+ to the stoichiometric countermovement of Cl−. E148 (Gluex) transfers protons between extracellular water and the protein interior, and E203 (Gluin) is thought to function analogously on the intracellular face of the protein. Mutation of either residue eliminates H+ transport while preserving Cl− transport. We tested the role of Gluin by examining structural and functional properties of mutants at this position. Certain dissociable side chains (E, D, H, K, R, but not C and Y) retain H+/Cl− exchanger activity to varying degrees, while other mutations (V, I, or C) abolish H+ coupling and severely inhibit Cl− flux. Transporters substituted with other nonprotonatable side chains (Q, S, and A) show highly impaired H+ transport with substantial Cl− transport. Influence on H+ transport of side chain length and acidity was assessed using a single-cysteine mutant to introduce non-natural side chains. Crystal structures of both coupled (E203H) and uncoupled (E203V) mutants are similar to wild type. The results support the idea that Gluin is the internal proton-transfer residue that delivers protons from intracellular solution to the protein interior, where they couple to Cl− movements to bring about Cl−/H+ exchange.

Evaluation of the Functional Role of the Heme-6-propionate Side Chain in Cytochrome P450cam

2008 ◽  
Vol 130 (2) ◽  
pp. 432-433 ◽  
Author(s):  
Katsuyoshi Harada ◽  
Keisuke Sakurai ◽  
Kenichiro Ikemura ◽  
Takashi Ogura ◽  
Shun Hirota ◽  
...  
Keyword(s):  
Functional Role ◽  
Side Chain ◽  
Cytochrome P450cam
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