Bacterial Oxidases of the Cytochrome bd Family: Redox Enzymes of Unique Structure, Function, and Utility As Drug Targets

VB Borisov, SA Siletsky, A Paiardini… - Antioxidants & redox …, 2021 - liebertpub.com
Significance: Cytochrome bd is a ubiquinol: oxygen oxidoreductase of many prokaryotic
respiratory chains with a unique structure and functional characteristics. Its primary role is to …

Heme cross-feeding can augment Staphylococcus aureus and Enterococcus faecalis dual species biofilms

JH Ch'ng, M Muthu, KKL Chong, JJ Wong… - The ISME …, 2022 - academic.oup.com
The contribution of biofilms to virulence and as a barrier to treatment is well-established for
Staphylococcus aureus and Enterococcus faecalis, both nosocomial pathogens frequently …

The CydDC ABC transporter of Escherichia coli: new roles for a reductant efflux pump

M Shepherd - Biochemical Society Transactions, 2015 - portlandpress.com
The CydDC complex of Escherichia coli is a heterodimeric ATP-binding cassette (ABC)
transporter that exports cysteine and glutathione to the periplasm. These reductants are …

Profiling the Heme‐Binding Proteomes of Bacteria Using Chemical Proteomics

IVL Wilkinson, M Bottlinger… - Angewandte Chemie …, 2023 - Wiley Online Library
Heme is a cofactor with myriad roles and essential to almost all living organisms. Beyond
classical gas transport and catalytic functions, heme is increasingly appreciated as a tightly …

A heme-binding domain controls regulation of ATP-dependent potassium channels

MJ Burton, SM Kapetanaki, T Chernova… - Proceedings of the …, 2016 - pnas.org
Heme iron has many and varied roles in biology. Most commonly it binds as a prosthetic
group to proteins, and it has been widely supposed and amply demonstrated that subtle …

A role for PchHI as the ABC transporter in iron acquisition by the siderophore pyochelin in Pseudomonas aeruginosa

B Roche, MA Garcia‐Rivera, V Normant… - Environmental …, 2022 - Wiley Online Library
Iron is an essential nutrient for bacterial growth but poorly bioavailable. Bacteria scavenge
ferric iron by synthesizing and secreting siderophores, small compounds with a high affinity …

Dissecting the conformational complexity and mechanism of a bacterial heme transporter

D Wu, AR Mehdipour, F Finke, HG Goojani… - Nature Chemical …, 2023 - nature.com
Iron-bound cyclic tetrapyrroles (hemes) are redox-active cofactors in bioenergetic enzymes.
However, the mechanisms of heme transport and insertion into respiratory chain complexes …

CydDC-mediated reductant export in Escherichia coli controls the transcriptional wiring of energy metabolism and combats nitrosative stress

LV Holyoake, S Hunt, G Sanguinetti… - Biochemical …, 2016 - portlandpress.com
The glutathione/cysteine exporter CydDC maintains redox balance in Escherichia coli. A
cydD mutant strain was used to probe the influence of CydDC upon reduced thiol export …

Restoration of biofuel production levels and increased tolerance under ionic liquid stress is enabled by a mutation in the essential Escherichia coli gene cydC

T Eng, P Demling, RA Herbert, Y Chen, V Benites… - Microbial cell …, 2018 - Springer
Background Microbial production of chemicals from renewable carbon sources enables a
sustainable route to many bioproducts. Sugar streams, such as those derived from biomass …

CydDC functions as a cytoplasmic cystine reductase to sensitize Escherichia coli to oxidative stress and aminoglycosides

A Mironov, T Seregina, K Shatalin… - Proceedings of the …, 2020 - pnas.org
l-cysteine is the source of all bacterial sulfurous biomolecules. However, the cytoplasmic
level of l-cysteine must be tightly regulated due to its propensity to reduce iron and drive …