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Using Biosynthetic Models of Heme‐Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities
Author(s) -
BhagiDamodaran Ambika,
Petrik Igor,
Lu Yi
Publication year - 2016
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.201600033
Subject(s) - myoglobin , heme , nitric oxide , enzyme , chemistry , biochemistry , nitrite reductase , active site , organic chemistry , nitrate reductase
In biology, a heme‐Cu center in heme‐copper oxidases (HCOs) is used to catalyze the four‐electron reduction of oxygen to water, while a heme‐nonheme diiron center in nitric oxide reductases (NORs) is employed to catalyze the two‐electron reduction of nitric oxide to nitrous oxide. Although much progress has been made in biochemical and biophysical studies of HCOs and NORs, structural features responsible for similarities and differences within the two enzymatic systems remain to be understood. Here, we discuss the progress made in the design and characterization of myoglobin‐based enzyme models of HCOs and NORs. In particular, we focus on use of these models to understand the structure‐function relations between HCOs and NORs, including the role of nonheme metals, conserved amino acids in the active site, heme types, and hydrogen‐bonding networks, in tuning enzymatic activities and total turnovers. Insights gained from these studies are summarized and future directions are proposed.