Assembly and Function of the Bacillus anthracis S-Layer

D Missiakas, O Schneewind - Annual review of microbiology, 2017 - annualreviews.org
Bacillus anthracis, the anthrax agent, is a member of the Bacillus cereus sensu lato group,
which includes invasive pathogens of mammals or insects as well as nonpathogenic …

From host heme to iron: the expanding spectrum of heme degrading enzymes used by pathogenic bacteria

KV Lyles, Z Eichenbaum - Frontiers in cellular and infection …, 2018 - frontiersin.org
Iron is an essential nutrient for many bacteria. Since the metal is highly sequestered in host
tissues, bound predominantly to heme, pathogenic bacteria often take advantage of heme …

Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamily

B Goblirsch, RC Kurker, BR Streit, CM Wilmot… - Journal of molecular …, 2011 - Elsevier
Heme proteins are extremely diverse, widespread, and versatile biocatalysts, sensors, and
molecular transporters. The chlorite dismutase family of hemoproteins received its name due …

Nfu facilitates the maturation of iron‐sulfur proteins and participates in virulence in Staphylococcus aureus

AA Mashruwala, YY Pang, Z Rosario‐Cruz… - Molecular …, 2015 - Wiley Online Library
The acquisition and metabolism of iron (Fe) by the human pathogen S taphylococcus aureus
is critical for disease progression. S. aureus requires Fe to synthesize inorganic cofactors …

Structure–function analyses reveal key features in Staphylococcus aureus IsdB-associated unfolding of the heme-binding pocket of human hemoglobin

CFM Bowden, ACK Chan, EJW Li, AL Arrieta… - Journal of Biological …, 2018 - ASBMB
IsdB is a receptor on the surface of the bacterial pathogen Staphylococcus aureus that
extracts heme from hemoglobin (Hb) to enable growth on Hb as a sole iron source. IsdB is …

Recent advances in bacterial heme protein biochemistry

JA Mayfield, CA Dehner, JL DuBois - Current opinion in chemical biology, 2011 - Elsevier
Recent progress in genetics, fed by the burst in genome sequence data, has led to the
identification of a host of novel bacterial heme proteins that are now being characterized in …

The Escherichia coli protein YfeX functions as a porphyrinogen oxidase, not a heme dechelatase

HA Dailey, AN Septer, L Daugherty, D Thames… - MBio, 2011 - Am Soc Microbiol
ABSTRACT The protein YfeX from Escherichia coli has been proposed to be essential for
the process of iron removal from heme by carrying out a dechelation of heme without …

The theft of host heme by Gram-positive pathogenic bacteria

CL Nobles, AW Maresso - Metallomics, 2011 - academic.oup.com
The element iron is essential for bacteria and plays a key role in the virulence and pathology
of bacterial diseases. The largest reservoir of iron within the human body is in …

Measurement of heme ruffling changes in MhuD using UV–vis spectroscopy

AB Graves, MT Graves, MD Liptak - The Journal of Physical …, 2016 - ACS Publications
For decades it has been known that an out-of-plane ruffling distortion of heme perturbs its
UV–vis absorption (Abs) spectrum, but whether increased ruffling induces a red or blue shift …

Electronic properties of the highly ruffled heme bound to the heme degrading enzyme IsdI

SJ Takayama, G Ukpabi… - Proceedings of the …, 2011 - National Acad Sciences
IsdI, a heme-degrading protein from Staphylococcus aureus, binds heme in a manner that
distorts the normally planar heme prosthetic group to an extent greater than that observed so …