Classification and enzyme kinetics of formate dehydrogenases for biomanufacturing via CO2 utilization

Christian Førgaard Nielsen, Lene Lange, Anne S. Meyer*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The reversible interconversion of formate (HCOO) and carbon dioxide (CO2) is catalyzed by formate dehydrogenase (FDH, EC 1.17.1.9). This enzyme can be used as a first step in the utilization of CO2 as carbon substrate for production of high-in-demand chemicals. However, comparison and categorization of the very diverse group of FDH enzymes has received only limited attention. With specific emphasis on FDH catalyzed CO2 reduction to HCOO, we present a novel classification scheme for FDHs based on protein sequence alignment and gene organization analysis. We show that prokaryotic FDHs can be neatly divided into six meaningful sub-types. These sub-types are discussed in the context of overall structural composition, phylogeny of the gene segment organization, metabolic role, and catalytic properties of the enzymes. Based on the available literature, the influence of electron donor choice on the efficacy of FDH catalyzed CO2 reduction is quantified and compared. This analysis shows that methyl viologen and hydrogen are several times more potent than NADH as electron donors. Hence, the new FDH classification scheme and the electron donor analysis provide an improved base for developing FDH-facilitated CO2 reduction as a viable step in the utilization of CO2 as carbon source for green production of chemicals.

Original languageEnglish
Article number107408
JournalBiotechnology Advances
Number of pages11
ISSN0734-9750
DOIs
Publication statusAccepted/In press - 2019

Keywords

  • Biocatalysis
  • Carbon capture and utilization
  • CO reduction
  • Electrocatalysis
  • FDH classification
  • FDH gene segment organization
  • Formate

Cite this

@article{7499e3b70bc64257b1a61448dc1a8b07,
title = "Classification and enzyme kinetics of formate dehydrogenases for biomanufacturing via CO2 utilization",
abstract = "The reversible interconversion of formate (HCOO−) and carbon dioxide (CO2) is catalyzed by formate dehydrogenase (FDH, EC 1.17.1.9). This enzyme can be used as a first step in the utilization of CO2 as carbon substrate for production of high-in-demand chemicals. However, comparison and categorization of the very diverse group of FDH enzymes has received only limited attention. With specific emphasis on FDH catalyzed CO2 reduction to HCOO−, we present a novel classification scheme for FDHs based on protein sequence alignment and gene organization analysis. We show that prokaryotic FDHs can be neatly divided into six meaningful sub-types. These sub-types are discussed in the context of overall structural composition, phylogeny of the gene segment organization, metabolic role, and catalytic properties of the enzymes. Based on the available literature, the influence of electron donor choice on the efficacy of FDH catalyzed CO2 reduction is quantified and compared. This analysis shows that methyl viologen and hydrogen are several times more potent than NADH as electron donors. Hence, the new FDH classification scheme and the electron donor analysis provide an improved base for developing FDH-facilitated CO2 reduction as a viable step in the utilization of CO2 as carbon source for green production of chemicals.",
keywords = "Biocatalysis, Carbon capture and utilization, CO reduction, Electrocatalysis, FDH classification, FDH gene segment organization, Formate",
author = "Nielsen, {Christian F{\o}rgaard} and Lene Lange and Meyer, {Anne S.}",
year = "2019",
doi = "10.1016/j.biotechadv.2019.06.007",
language = "English",
journal = "Biotechnology Advances",
issn = "0734-9750",
publisher = "Elsevier",

}

Classification and enzyme kinetics of formate dehydrogenases for biomanufacturing via CO2 utilization. / Nielsen, Christian Førgaard; Lange, Lene; Meyer, Anne S.

In: Biotechnology Advances, 2019.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - Classification and enzyme kinetics of formate dehydrogenases for biomanufacturing via CO2 utilization

AU - Nielsen, Christian Førgaard

AU - Lange, Lene

AU - Meyer, Anne S.

PY - 2019

Y1 - 2019

N2 - The reversible interconversion of formate (HCOO−) and carbon dioxide (CO2) is catalyzed by formate dehydrogenase (FDH, EC 1.17.1.9). This enzyme can be used as a first step in the utilization of CO2 as carbon substrate for production of high-in-demand chemicals. However, comparison and categorization of the very diverse group of FDH enzymes has received only limited attention. With specific emphasis on FDH catalyzed CO2 reduction to HCOO−, we present a novel classification scheme for FDHs based on protein sequence alignment and gene organization analysis. We show that prokaryotic FDHs can be neatly divided into six meaningful sub-types. These sub-types are discussed in the context of overall structural composition, phylogeny of the gene segment organization, metabolic role, and catalytic properties of the enzymes. Based on the available literature, the influence of electron donor choice on the efficacy of FDH catalyzed CO2 reduction is quantified and compared. This analysis shows that methyl viologen and hydrogen are several times more potent than NADH as electron donors. Hence, the new FDH classification scheme and the electron donor analysis provide an improved base for developing FDH-facilitated CO2 reduction as a viable step in the utilization of CO2 as carbon source for green production of chemicals.

AB - The reversible interconversion of formate (HCOO−) and carbon dioxide (CO2) is catalyzed by formate dehydrogenase (FDH, EC 1.17.1.9). This enzyme can be used as a first step in the utilization of CO2 as carbon substrate for production of high-in-demand chemicals. However, comparison and categorization of the very diverse group of FDH enzymes has received only limited attention. With specific emphasis on FDH catalyzed CO2 reduction to HCOO−, we present a novel classification scheme for FDHs based on protein sequence alignment and gene organization analysis. We show that prokaryotic FDHs can be neatly divided into six meaningful sub-types. These sub-types are discussed in the context of overall structural composition, phylogeny of the gene segment organization, metabolic role, and catalytic properties of the enzymes. Based on the available literature, the influence of electron donor choice on the efficacy of FDH catalyzed CO2 reduction is quantified and compared. This analysis shows that methyl viologen and hydrogen are several times more potent than NADH as electron donors. Hence, the new FDH classification scheme and the electron donor analysis provide an improved base for developing FDH-facilitated CO2 reduction as a viable step in the utilization of CO2 as carbon source for green production of chemicals.

KW - Biocatalysis

KW - Carbon capture and utilization

KW - CO reduction

KW - Electrocatalysis

KW - FDH classification

KW - FDH gene segment organization

KW - Formate

U2 - 10.1016/j.biotechadv.2019.06.007

DO - 10.1016/j.biotechadv.2019.06.007

M3 - Journal article

JO - Biotechnology Advances

JF - Biotechnology Advances

SN - 0734-9750

M1 - 107408

ER -