Ribonucleotide reductase - Structural studies of a radical enzyme
Eklund, Hans ; Eriksson, Mathias ; Uhlin, Ulla ; Nordlund, Pär and Logan, Derek LU
(1997)
In Biological Chemistry
378(8).
p.821-825
- Abstract
Ribonucleotide reductase contains a stable organic free radical essential for its activity located on a tyrosine residue in the small subunit of the enzyme called R2. The substrate binding site is, however, found in the catalytic subunit called R1. A long-range protein-mediated radical transfer pathway appears to be responsible for the delivery of the radical from the tyrosine in R2 to the substrate on R1. The active site is located deep inside the protein in a very stable β/α-barrel structure and a hydrogen bonded system leads from the surface to Cys439 at the active site which is in excellent position to remove a hydrogen from the 3' of the ribose of a bound substrate nucleotide.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/9929c868-598a-4d3f-9bb7-87a6c2c97e89
- author
- Eklund, Hans
; Eriksson, Mathias
; Uhlin, Ulla
; Nordlund, Pär
and Logan, Derek
LU
- publishing date
- 1997-08
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Allosteric regulation, Di-iron protein, Radical transfer, Redox active cysteines, Substrate binding, Tyrosyl radical
- in
- Biological Chemistry
- volume
- 378
- issue
- 8
- pages
- 5 pages
- publisher
- De Gruyter
- external identifiers
-
- scopus:0030762177
- pmid:9377477
- ISSN
- 1431-6730
- DOI
- 10.1515/bchm.1997.378.8.815
- language
- English
- LU publication?
- no
- id
- 9929c868-598a-4d3f-9bb7-87a6c2c97e89
- date added to LUP
- 2022-04-25 11:27:00
- date last changed
- 2024-01-03 10:38:05
@article{9929c868-598a-4d3f-9bb7-87a6c2c97e89,
abstract = {{<p>Ribonucleotide reductase contains a stable organic free radical essential for its activity located on a tyrosine residue in the small subunit of the enzyme called R2. The substrate binding site is, however, found in the catalytic subunit called R1. A long-range protein-mediated radical transfer pathway appears to be responsible for the delivery of the radical from the tyrosine in R2 to the substrate on R1. The active site is located deep inside the protein in a very stable β/α-barrel structure and a hydrogen bonded system leads from the surface to Cys439 at the active site which is in excellent position to remove a hydrogen from the 3' of the ribose of a bound substrate nucleotide.</p>}},
author = {{Eklund, Hans and Eriksson, Mathias and Uhlin, Ulla and Nordlund, Pär and Logan, Derek}},
issn = {{1431-6730}},
keywords = {{Allosteric regulation; Di-iron protein; Radical transfer; Redox active cysteines; Substrate binding; Tyrosyl radical}},
language = {{eng}},
number = {{8}},
pages = {{821--825}},
publisher = {{De Gruyter}},
series = {{Biological Chemistry}},
title = {{Ribonucleotide reductase - Structural studies of a radical enzyme}},
url = {{http://dx.doi.org/10.1515/bchm.1997.378.8.815}},
doi = {{10.1515/bchm.1997.378.8.815}},
volume = {{378}},
year = {{1997}},
}