Determinants of Ligand Affinity and Heme Reactivity in H‐NOX Domains | Zendy

Weinert Emily E. | Zendy; Plate Lars | Zendy; Whited Charlotte A. | Zendy; Olea Charles | Zendy; Marletta Michael A. | Zendy

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Determinants of Ligand Affinity and Heme Reactivity in H‐NOX Domains

Author(s) -

Weinert Emily E.,

Plate Lars,

Whited Charlotte A.,

Olea Charles,

Marletta Michael A.

Publication year - 2010

Publication title -

angewandte chemie international edition

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.831

H-Index - 550

eISSN - 1521-3773

pISSN - 1433-7851

DOI - 10.1002/anie.200904799

Subject(s) - heme , chemistry , reactivity (psychology) , ligand (biochemistry) , nitric oxide , kinetics , nox , hemeprotein , stereochemistry , biochemistry , biophysics , receptor , biology , enzyme , organic chemistry , physics , medicine , alternative medicine , pathology , quantum mechanics , combustion

O 2 balks at extra bulk : The introduction of distal‐pocket bulk into the Thermoanaerobacter tengcongensis H‐NOX (heme nitric oxide/oxygen) domain caused key changes in the protein structure. Rearrangement of the heme pocket resulted in dramatic differences in O 2 ‐binding kinetics and heme reactivity (see picture).

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