Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities

Ambika Bhagi-Damodaran, Igor Petrik, Yi Lu

Research output: Contribution to journalReview article

Abstract

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.

Original languageEnglish (US)
Pages (from-to)773-790
Number of pages18
JournalIsrael Journal of Chemistry
Volume56
Issue number9-10
DOIs
StatePublished - Oct 1 2016

Fingerprint

Myoglobin
Heme
Electrons
Nitrous Oxide
copper oxidase
nitric-oxide reductase
Hydrogen bonds
Nitric Oxide
Tuning
Metals
Oxygen
Amino Acids
Water
Enzymes

Keywords

  • amino acids
  • enzymes
  • heme-copper oxidases
  • nitric oxide reductases

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities. / Bhagi-Damodaran, Ambika; Petrik, Igor; Lu, Yi.

In: Israel Journal of Chemistry, Vol. 56, No. 9-10, 01.10.2016, p. 773-790.

Research output: Contribution to journalReview article

@article{9f48bf66b516476b9cd8671322718d19,
title = "Using Biosynthetic Models of Heme-Copper Oxidase and Nitric Oxide Reductase in Myoglobin to Elucidate Structural Features Responsible for Enzymatic Activities",
abstract = "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.",
keywords = "amino acids, enzymes, heme-copper oxidases, nitric oxide reductases",
author = "Ambika Bhagi-Damodaran and Igor Petrik and Yi Lu",
year = "2016",
month = "10",
day = "1",
doi = "10.1002/ijch.201600033",
language = "English (US)",
volume = "56",
pages = "773--790",
journal = "Israel Journal of Chemistry",
issn = "0021-2148",
publisher = "Wiley-VCH Verlag",
number = "9-10",

}

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

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

UR - http://www.scopus.com/inward/record.url?scp=84987926910&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84987926910&partnerID=8YFLogxK

U2 - 10.1002/ijch.201600033

DO - 10.1002/ijch.201600033

M3 - Review article

AN - SCOPUS:84987926910

VL - 56

SP - 773

EP - 790

JO - Israel Journal of Chemistry

JF - Israel Journal of Chemistry

SN - 0021-2148

IS - 9-10

ER -