Results 31 to 40 of about 428,654 (353)
From Synthesis to Utilization: The Ins and Outs of Mitochondrial Heme
Cells, 2020 Heme is a ubiquitous and essential iron containing metallo-organic cofactor required for virtually all aerobic life. Heme synthesis is initiated and completed in mitochondria, followed by certain covalent modifications and/or its delivery to apo ...
Samantha A. Swenson +5 more
semanticscholar +1 more source
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
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
Frontiers in Microbiology, 2021 Iron is an important micronutrient that is required by bacteria to proliferate and to cause disease. Many bacterial pathogens forage iron from human hemoglobin (Hb) during infections, which contains this metal within heme (iron–protoporphyrin IX ...
Ken Ellis-Guardiola +6 more
doaj +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
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
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
Nitric oxide binds to the proximal heme coordination site of the ferrocytochrome c/cardiolipin complex: formation mechanism and dynamics. [PDF]
, 2010 Mammalian mitochondrial cytochrome c interacts with cardiolipin to form a complex (cyt. c/CL) important in apoptosis. Here we show that this interaction leads to structural changes in ferrocytochrome c that leads to an open coordinate site on the central
Husu, I +4 more
core +4 more sources
A Dual Role of Heme Oxygenase-1 in Cancer Cells
International Journal of Molecular Sciences, 2018 Heme oxygenase (HO)-1 is known to metabolize heme into biliverdin/bilirubin, carbon monoxide, and ferrous iron, and it has been suggested to demonstrate cytoprotective effects against various stress-related conditions.
Shih-Kai Chiang +2 more
semanticscholar +1 more source