TY - JOUR
T1 - Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities
AU - Bhagi-Damodaran, Ambika
AU - Petrik, Igor
AU - Lu, Yi
N1 - Publisher Copyright:
© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
PY - 2016/10/1
Y1 - 2016/10/1
N2 - 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.
AB - 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.
KW - amino acids
KW - enzymes
KW - heme-copper oxidases
KW - nitric oxide reductases
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U2 - 10.1002/ijch.201600033
DO - 10.1002/ijch.201600033
M3 - Review article
AN - SCOPUS:84987926910
SN - 0021-2148
VL - 56
SP - 773
EP - 790
JO - Israel Journal of Chemistry
JF - Israel Journal of Chemistry
IS - 9-10
ER -