Discovering How Heme Controls Genome Function Through Heme-omics
Cell Reports, 2020 Summary: Protein ensembles control genome function by establishing, maintaining, and deconstructing cell-type-specific chromosomal landscapes. A plethora of small molecules orchestrate cellular functions and therefore may link physiological processes ...
Ruiqi Liao +12 more
doaj +1 more source
Heme iron from meat and risk of colorectal cancer: a meta-analysis and a review of the mechanisms involved [PDF]
, 2011 Red meat and processed meat intake is associated with a risk of colorectal cancer, a major cause of death in affluent countries. Epidemiological and experimental evidence supports the hypothesis that heme iron present in meat promotes colorectal cancer ...
Bingham +24 more
core +4 more sources
Regulation of nitric oxide signaling by formation of a distal receptor-ligand complex. [PDF]
, 2017 The binding of nitric oxide (NO) to the heme cofactor of heme-nitric oxide/oxygen binding (H-NOX) proteins can lead to the dissociation of the heme-ligating histidine residue and yield a five-coordinate nitrosyl complex, an important step for NO ...
Britt, R David +5 more
core +1 more source
Antioxidants, 2020 SARS-CoV-2 is causing a pandemic resulting in high morbidity and mortality. COVID-19 patients suffering from acute respiratory distress syndrome (ARDS) are often critically ill and show lung injury and hemolysis.
F. Wagener +4 more
semanticscholar +1 more source
Control of intracellular heme levels: Heme transporters and heme oxygenases
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, 2011 Heme serves as a co-factor in proteins involved in fundamental biological processes including oxidative metabolism, oxygen storage and transport, signal transduction and drug metabolism. In addition, heme is important for systemic iron homeostasis in mammals.
Anwar A. Khan, John G. Quigley
openaire +3 more sources
Multi-heme Cytochromes in Shewanella oneidensis MR-1:Structures, functions and opportunities [PDF]
, 2015 Multi-heme cytochromes are employed by a range of microorganisms to transport electrons over distances of up to tens of nanometers. Perhaps the most spectacular utilization of these proteins is in the reduction of extracellular solid substrates ...
Brown JP +9 more
core +1 more source
Structure-Guided Recombination Creates an Artificial Family of Cytochromes P450 [PDF]
, 2006 Creating artificial protein families affords new opportunities to explore the determinants of structure and biological function free from many of the constraints of natural selection.
Arnold, Frances H. +5 more
core +1 more source
Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins
Chemical Reviews, 2017 As a result of the adaptation of life to an aerobic environment, nature has evolved a panoply of metalloproteins for oxidative metabolism and protection against reactive oxygen species. Despite the diverse structures and functions of these proteins, they
Xiong Huang, J. Groves
semanticscholar +1 more source
Heme Oxygenase-2 Is a Hemoprotein and Binds Heme through Heme Regulatory Motifs That Are Not Involved in Heme Catalysis [PDF]
Journal of Biological Chemistry, 1997 The heme oxygenase (HO) system degrades heme to biliverdin and CO and releases chelated iron. In the primary sequence of the constitutive form, HO-2, there are three potential heme binding sites: two heme regulatory motifs (HRMs) with the absolutely conserved Cys-Pro pair, and a conserved 24-residue heme catalytic pocket with a histidine residue ...
Tian J. Huang +2 more
openaire +3 more sources
mBio, 2018 Staphylococcus aureus is responsible for a significant amount of devastating disease. Its ability to colonize the host and cause infection is supported by a variety of proteins that are dependent on the cofactor heme.
Jacob E. Choby +5 more
doaj +1 more source