Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase

C. Kent Brown, Matthew W. Vetting, Cathleen A. Earhart, Douglas H. Ohlendorf

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3- dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

Original languageEnglish (US)
Pages (from-to)555-585
Number of pages31
JournalAnnual Review of Microbiology
Volume58
DOIs
StatePublished - 2004

Fingerprint

Protocatechuate-3,4-Dioxygenase
Dioxygenases
Enzymes
Carbon
Iron
Metals
Ions
Bacteria
catechol

Keywords

  • Catechol
  • Crystallography
  • Dioxygenase
  • Iron
  • Metalloenzyme
  • Protocatechuate

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase. / Brown, C. Kent; Vetting, Matthew W.; Earhart, Cathleen A.; Ohlendorf, Douglas H.

In: Annual Review of Microbiology, Vol. 58, 2004, p. 555-585.

Research output: Contribution to journalArticle

Brown, C. Kent ; Vetting, Matthew W. ; Earhart, Cathleen A. ; Ohlendorf, Douglas H. / Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase. In: Annual Review of Microbiology. 2004 ; Vol. 58. pp. 555-585.
@article{621f7812eb7f461192564b556c0a4257,
title = "Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase",
abstract = "The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3- dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.",
keywords = "Catechol, Crystallography, Dioxygenase, Iron, Metalloenzyme, Protocatechuate",
author = "Brown, {C. Kent} and Vetting, {Matthew W.} and Earhart, {Cathleen A.} and Ohlendorf, {Douglas H.}",
year = "2004",
doi = "10.1146/annurev.micro.57.030502.090927",
language = "English (US)",
volume = "58",
pages = "555--585",
journal = "Annual Review of Microbiology",
issn = "0066-4227",
publisher = "Annual Reviews Inc.",

}

TY - JOUR

T1 - Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase

AU - Brown, C. Kent

AU - Vetting, Matthew W.

AU - Earhart, Cathleen A.

AU - Ohlendorf, Douglas H.

PY - 2004

Y1 - 2004

N2 - The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3- dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

AB - The catechol dioxygenases allow a wide variety of bacteria to use aromatic compounds as carbon sources by catalyzing the key ring-opening step. These enzymes use specifically either catechol or protocatechuate (2,3- dihydroxybenozate) as their substrates; they use a bare metal ion as the sole cofactor. To learn how this family of metalloenzymes functions, a structural analysis of designed and selected mutants of these enzymes has been undertaken. Here we review the results of this analysis on the nonheme ferric iron intradiol dioxygenase protocatechuate 3,4-dioxygenase.

KW - Catechol

KW - Crystallography

KW - Dioxygenase

KW - Iron

KW - Metalloenzyme

KW - Protocatechuate

UR - http://www.scopus.com/inward/record.url?scp=9244231291&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=9244231291&partnerID=8YFLogxK

U2 - 10.1146/annurev.micro.57.030502.090927

DO - 10.1146/annurev.micro.57.030502.090927

M3 - Article

C2 - 15487948

AN - SCOPUS:9244231291

VL - 58

SP - 555

EP - 585

JO - Annual Review of Microbiology

JF - Annual Review of Microbiology

SN - 0066-4227

ER -