Heme-containing Dioxygenases

Igor Efimov; Jaswir Basran; Sarah J. Thackray; Sandeep Handa; Christopher G. Mowat; Emma Lloyd Raven

doi:10.1016/B978-0-12-396462-5.00002-7

Heme-containing Dioxygenases

Igor Efimov^*, Jaswir Basran, Sarah J. Thackray, Sandeep Handa, Christopher G. Mowat, Emma Lloyd Raven

^*Corresponding author for this work

School of Chemistry

Research output: Contribution to journal › Article (Academic Journal) › peer-review

4 Citations (Scopus)

Abstract

The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway-the O ₂-dependent oxidation of l-tryptophan to N-formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a number of dioxygenases, contributions from computational chemistry, and emerging mechanistic data from site-directed mutagenesis. This review summarizes these recent contributions.

Original language	English
Pages (from-to)	33-51
Number of pages	19
Journal	Advances in Inorganic Chemistry
Volume	64
DOIs	https://doi.org/10.1016/B978-0-12-396462-5.00002-7
Publication status	Published - 5 Mar 2012

Keywords

Dioxygenases
Heme
Iron

Access to Document

10.1016/B978-0-12-396462-5.00002-7

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@article{4466533c83434c719de1bee794a0939a,

title = "Heme-containing Dioxygenases",

abstract = "The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway-the O 2-dependent oxidation of l-tryptophan to N-formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a number of dioxygenases, contributions from computational chemistry, and emerging mechanistic data from site-directed mutagenesis. This review summarizes these recent contributions.",

keywords = "Dioxygenases, Heme, Iron",

author = "Igor Efimov and Jaswir Basran and Thackray, {Sarah J.} and Sandeep Handa and Mowat, {Christopher G.} and Raven, {Emma Lloyd}",

year = "2012",

month = mar,

day = "5",

doi = "10.1016/B978-0-12-396462-5.00002-7",

language = "English",

volume = "64",

pages = "33--51",

journal = "Advances in Inorganic Chemistry",

issn = "0898-8838",

publisher = "Elsevier Inc.",

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TY - JOUR

T1 - Heme-containing Dioxygenases

AU - Efimov, Igor

AU - Basran, Jaswir

AU - Thackray, Sarah J.

AU - Handa, Sandeep

AU - Mowat, Christopher G.

AU - Raven, Emma Lloyd

PY - 2012/3/5

Y1 - 2012/3/5

N2 - The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway-the O 2-dependent oxidation of l-tryptophan to N-formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a number of dioxygenases, contributions from computational chemistry, and emerging mechanistic data from site-directed mutagenesis. This review summarizes these recent contributions.

AB - The heme dioxygenase enzymes involved in tryptophan oxidation catalyse the first and rate-limiting step in the kynurenine pathway-the O 2-dependent oxidation of l-tryptophan to N-formylkynurenine. In the past 10 years, there have been substantial new developments, including new structural information, bacterial expression systems for a number of dioxygenases, contributions from computational chemistry, and emerging mechanistic data from site-directed mutagenesis. This review summarizes these recent contributions.

KW - Dioxygenases

KW - Heme

KW - Iron

UR - http://www.scopus.com/inward/record.url?scp=84857601269&partnerID=8YFLogxK

U2 - 10.1016/B978-0-12-396462-5.00002-7

DO - 10.1016/B978-0-12-396462-5.00002-7

M3 - Article (Academic Journal)

AN - SCOPUS:84857601269

VL - 64

SP - 33

EP - 51

JO - Advances in Inorganic Chemistry

JF - Advances in Inorganic Chemistry

SN - 0898-8838

ER -