OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường
Duyệt OER - Kỹ thuật hóa học; Công nghệ sinh học - Thực phẩm; Công nghệ môi trường theo Chủ đề "2Fe-2S"
Ấn phẩm
The structure of a novel ferredoxin – FhuF, a ferric-siderophore reductase from E. coli K-12 with a novel 2Fe-2S cluster coordination
Iron is a vital element for life. However, after the Great Oxidation
Event, the bioavailability of this element became limited. To overcome iron
shortage and to scavenge this essential nutrient, microorganisms use
siderophores, secondary metabolites that have some of the highest affinities
for ferric iron. The crucial step of iron release from these compounds to be
subsequently integrated into cellular components is mediated by Siderophore-
Interacting Proteins (SIPs) or Ferric-siderophore reductases (FSRs).
In this work, we report the structure of an FSR for the first time. FhuF
from laboratory strain Escherichia coli K-12 is the archetypical FSR, known for
its atypical 2Fe-2S cluster with the binding motif C-C-X10-C-X2-C. The 1.9 Å
resolution crystallographic structure of FhuF shows it to be the only 2Fe-2S
protein known to date with two consecutive cysteines binding different Fe
atoms. This novel coordination provides a rationale for the unusual
spectroscopic properties of FhuF. Furthermore, FhuF shows an impressive
ability to reduce hydroxamate-type siderophores at very high rates when
compared to flavin-based SIPs, but like SIPs it appears to use the redox-Bohr effect to achieve catalytic efficiency