TY - JOUR
T1 - Molecular understanding of heteronuclear active sites in heme-copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling
AU - Reed, Christopher J.
AU - Lam, Quan N.
AU - Mirts, Evan N.
AU - Lu, Yi
N1 - Funding Information:
The Lu group research described in this review has been supported by the National Institute of General Medical Sciences of the National Institutes of Health under award number GM062211 and Department of Energy's Center for Advanced Bioenergy and Bioproducts Innovation (Office of Science, Office of Biological and Environmental Research, under award DE-SC0018420). C. R. would like to acknowledge support from the National Institutes of Health Postdoctoral Fellowship (GM136177). We thank our group members and collaborators who have contributed to the results and insights gained from our studies. Q. L. would like to thank the National Science Foundation Graduate Research Fellowship Program for their support.
Publisher Copyright:
© The Royal Society of Chemistry 2021.
PY - 2021/2/21
Y1 - 2021/2/21
N2 - Heme-copper oxidases (HCO), nitric oxide reductases (NOR), and sulfite reductases (SiR) catalyze the multi-electron and multi-proton reductions of O2, NO, and SO32−, respectively. Each of these reactions is important to drive cellular energy production through respiratory metabolism and HCO, NOR, and SiR evolved to contain heteronuclear active sites containing heme/copper, heme/nonheme iron, and heme-[4Fe-4S] centers, respectively. The complexity of the structures and reactions of these native enzymes, along with their large sizes and/or membrane associations, make it challenging to fully understand the crucial structural features responsible for the catalytic properties of these active sites. In this review, we summarize progress that has been made to better understand these heteronuclear metalloenzymes at the molecular level though study of the native enzymes along with insights gained from biomimetic models comprising either small molecules or proteins. Further understanding the reaction selectivity of these enzymes is discussed through comparisons of their similar heteronuclear active sites, and we offer outlook for further investigations.
AB - Heme-copper oxidases (HCO), nitric oxide reductases (NOR), and sulfite reductases (SiR) catalyze the multi-electron and multi-proton reductions of O2, NO, and SO32−, respectively. Each of these reactions is important to drive cellular energy production through respiratory metabolism and HCO, NOR, and SiR evolved to contain heteronuclear active sites containing heme/copper, heme/nonheme iron, and heme-[4Fe-4S] centers, respectively. The complexity of the structures and reactions of these native enzymes, along with their large sizes and/or membrane associations, make it challenging to fully understand the crucial structural features responsible for the catalytic properties of these active sites. In this review, we summarize progress that has been made to better understand these heteronuclear metalloenzymes at the molecular level though study of the native enzymes along with insights gained from biomimetic models comprising either small molecules or proteins. Further understanding the reaction selectivity of these enzymes is discussed through comparisons of their similar heteronuclear active sites, and we offer outlook for further investigations.
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U2 - 10.1039/d0cs01297a
DO - 10.1039/d0cs01297a
M3 - Review article
C2 - 33475096
SN - 0306-0012
VL - 50
SP - 2486
EP - 2539
JO - Chemical Society Reviews
JF - Chemical Society Reviews
IS - 4
ER -