Results 181 to 190 of about 213,829 (198)
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Heme biosynthesis and trafficking
Free Radical Biology and Medicine, 2018Heme is an essential cofactor involved in a plethora of vital functions. Heme is required to be in most subcellular compartments, but the way, in which it is transported from the mitochondria - its site of synthesis - to those compartments is poorly understood.
Jonathan Dietz +5 more
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Heme Trafficking and the Importance of Handling Nature’s Most Versatile Cofactor
Chemical ReviewsHeme is one of the most versatile cofactors in nature from its role in oxygen transport and sensing, bioenergetics, and enzyme catalysis and is therefore an ideal regulatory molecule in responding to the redox status of the cell. However, due to both its redox reactivity and hydrophobicity, heme requires tight regulation at the level of its synthesis ...
Angela Wilks
exaly +3 more sources
Journal of Biological Inorganic Chemistry, 2015
C. elegans is a heme auxotroph that requires environmental heme for sustenance. As such, worms utilize HRG-3, a small heme-trafficking protein, to traffic heme from the intestine to extra-intestinal tissues and embryos. However, how HRG-3 binds and delivers heme remains unknown.
Sharon Ruthstein +2 more
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C. elegans is a heme auxotroph that requires environmental heme for sustenance. As such, worms utilize HRG-3, a small heme-trafficking protein, to traffic heme from the intestine to extra-intestinal tissues and embryos. However, how HRG-3 binds and delivers heme remains unknown.
Sharon Ruthstein +2 more
exaly +3 more sources
Biochemistry, 2007
PhuS is a cytoplasmic, 39 kDa heme-binding protein from Pseudomonas aeruginosa. It has previously been shown to transfer heme to its cognate heme oxygenase. It is expressed from the phu operon, which encodes a group of proteins known to actively internalize and transport heme from host organisms. This study combines the spectral resolution of resonance
Darci R, Block +5 more
openaire +2 more sources
PhuS is a cytoplasmic, 39 kDa heme-binding protein from Pseudomonas aeruginosa. It has previously been shown to transfer heme to its cognate heme oxygenase. It is expressed from the phu operon, which encodes a group of proteins known to actively internalize and transport heme from host organisms. This study combines the spectral resolution of resonance
Darci R, Block +5 more
openaire +2 more sources
Critical Reviews in Biochemistry and Molecular Biology, 2021
Michael Feig, Lim Heo, Eric L Hegg
exaly
Michael Feig, Lim Heo, Eric L Hegg
exaly
Porphyrin and Heme Trafficking in Metazoans
2013Iqbal Hamza, Harry A. Dailey
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Biophysical Perspectives on the Acquisition, Transport, and Trafficking of Heme in Bacteria
2013Kenton R. Rodgers +1 more
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Handling Heme: The Mechanisms Underlying the Movement of Heme Within and Between Cells
Free Radical Biology and Medicine, 2019Courtney M Moore, Amit R Reddi
exaly

