Results 41 to 50 of about 11,485 (176)

The Cytoplasmic Heme-binding Protein (PhuS) from the Heme Uptake System of Pseudomonas aeruginosa Is an Intracellular Heme-trafficking Protein to the δ-Regioselective Heme Oxygenase [PDF]

Journal of Biological Chemistry, 2006
The uptake and utilization of heme as an iron source is a receptor-mediated process in bacterial pathogens and involves a number of proteins required for internalization and degradation of heme. In the following report we provide the first in-depth spectroscopic and functional characterization of a cytoplasmic heme-binding protein PhuS from the ...
Ila B, Lansky, Gudrun S, Lukat-Rodgers, Darci, Block, Kenton R, Rodgers, Melanie, Ratliff, Angela, Wilks   +5 more
openaire   +2 more sources

Genes important for catalase activity in Enterococcus faecalis. [PDF]

PLoS ONE, 2012
Little in general is known about how heme proteins are assembled from their constituents in cells. The Gram-positive bacterium Enterococcus faecalis cannot synthesize heme and does not depend on it for growth.
Michael Baureder, Lars Hederstedt
doaj   +1 more source

The Role of the Cytoplasmic Heme-binding Protein (PhuS) of Pseudomonas aeruginosa in Intracellular Heme Trafficking and Iron Homeostasis [PDF]

Journal of Biological Chemistry, 2009
The cytoplasmic heme-binding protein PhuS, encoded within the Fur-regulated Pseudomonas heme utilization (phu) operon, has previously been shown to traffic heme to the iron-regulated heme oxygenase (HO). We further investigate the role of PhuS in heme trafficking to HO on disruption of the phuS and hemO genes in a Pseudomonas aeruginosa siderophore ...
Ajinder P, Kaur, Ila B, Lansky, Angela, Wilks   +2 more
openaire   +2 more sources

Structural and Functional Siderophore Remodeling by Enzymatic Delipidation

Angewandte Chemie, EarlyView.
A surprising functional switch in bacterial siderophores was discovered through genome mining and the analysis of environmental and pathogenic Pandoraea species. Pandorachelin B, a lipocyclopeptide that promotes swarming motility, is cleaved by a specialized acylase, yielding a ring‐contracted, homodetic cyclopeptide, pandorachelin A, which exhibits ...
Elena Herzog, Keishi Ishida, Evelyn M. Molloy, Ron Hermenau, Kirstin Scherlach, Christian Hertweck   +5 more
wiley   +2 more sources

Cj1386 is an ankyrin-containing protein involved in heme trafficking to catalase in Campylobacter jejuni. [PDF]

J Bacteriol, 2012
ABSTRACT Campylobacter jejuni , a microaerophilic bacterium, is the most frequent cause of human bacterial gastroenteritis. C. jejuni is exposed to harmful reactive oxygen species (ROS) produced during its own normal metabolic processes and during infection from the host immune system and from ...
Flint A, Sun YQ, Stintzi A.
europepmc   +4 more sources

Iron-tracking strategies: Chaperones capture iron in the cytosolic labile iron pool

Frontiers in Molecular Biosciences, 2023
Cells express hundreds of iron-dependent enzymes that rely on the iron cofactors heme, iron-sulfur clusters, and mono-or di-nuclear iron centers for activity.
Caroline C. Philpott, Olga Protchenko, Yubo Wang, Lorena Novoa-Aponte, Andres Leon-Torres, Samantha Grounds, Amber J. Tietgens   +6 more
doaj   +1 more source

Disruption of monocyte-macrophage differentiation and trafficking by a heme analog during active inflammation

Mucosal Immunology, 2022
Heme metabolism is a key regulator of inflammatory responses. Cobalt protoporphyrin IX (CoPP) is a heme analog and mimic that potently activates the NRF2/heme oxygenase-1 (HO-1) pathway, especially in monocytes and macrophages. We investigated the influence of CoPP on inflammatory responses using a murine model of colitis.
Rachel E.M. Schaefer, Rosemary C. Callahan, Shaikh M. Atif, David J. Orlicky, Ian M. Cartwright, Andrew P. Fontenot, Sean P. Colgan, Joseph C. Onyiah   +7 more
openaire   +2 more sources

One ring to rule them all: Trafficking of heme and heme synthesis intermediates in the metazoans

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2012
The appearance of heme, an organic ring surrounding an iron atom, in evolution forever changed the efficiency with which organisms were able to generate energy, utilize gasses and catalyze numerous reactions. Because of this, heme has become a near ubiquitous compound among living organisms.
Hamza, Iqbal, Dailey, Harry A.
openaire   +2 more sources

The sGC stimulator BAY-747 and activator runcaciguat can enhance memory in vivo via differential hippocampal plasticity mechanisms

Scientific Reports, 2022
Soluble guanylate cyclase (sGC) requires a heme-group bound in order to produce cGMP, a second messenger involved in memory formation, while heme-free sGC is inactive.
Ellis Nelissen, Nina Possemis, Nick P. Van Goethem, Melissa Schepers, Danielle A. J. Mulder-Jongen, Lisa Dietz, Wiebke Janssen, Michael Gerisch, Jörg Hüser, Peter Sandner, Tim Vanmierlo, Jos Prickaerts   +11 more
doaj   +1 more source

Biochemical mapping reveals a conserved heme transport mechanism via CcmCD in System I bacterial cytochrome c biogenesis

mBio
Heme is a redox-active cofactor for essential processes across all domains of life. Heme’s redox capabilities are responsible for its biological significance but also make it highly cytotoxic, requiring tight intracellular regulation.
Alicia N. Kreiman, Sarah E. Garner, Susan C. Carroll, Molly C. Sutherland   +3 more
doaj   +1 more source