User profiles for Harry A. Dailey
 | Harry A DaileyProfessor Emeritus, University of Georgia Verified email at uga.edu Cited by 9650 |
Prokaryotic heme biosynthesis: multiple pathways to a common essential product
The advent of heme during evolution allowed organisms possessing this compound to
safely and efficiently carry out a variety of chemical reactions that otherwise were difficult or …
safely and efficiently carry out a variety of chemical reactions that otherwise were difficult or …
[HTML][HTML] One ring to rule them all: trafficking of heme and heme synthesis intermediates in the metazoans
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 …
changed the efficiency with which organisms were able to generate energy, utilize gasses and …
Human ferrochelatase is an iron-sulfur protein
HA Dailey, MG Finnegan, MK Johnson - Biochemistry, 1994 - ACS Publications
MATERIALS AND METHODS Recombinant human ferrochelatase and the carboxyl-terminal
truncated version of the enzyme were produced and purified as described previously (…
truncated version of the enzyme were produced and purified as described previously (…
The 2.0 Å structure of human ferrochelatase, the terminal enzyme of heme biosynthesis
Human ferrochelatase (EC 4.99. 1.1) is a homodimeric (86 kDa) mitochondrial membrane-associated
enzyme that catalyzes the insertion of ferrous iron into protoporphyrin to form heme…
enzyme that catalyzes the insertion of ferrous iron into protoporphyrin to form heme…
A R59W mutation in human protoporphyrinogen oxidase results in decreased enzyme activity and is prevalent in South Africans with variegate porphyria
Variegate porphyria (VP), a low-penetrant autosomal dominant inherited disorder of haem
metabolism, is characterised by photosensitivity (Fig. 1) and a propensity to develop acute …
metabolism, is characterised by photosensitivity (Fig. 1) and a propensity to develop acute …
Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis
W Chen, HA Dailey, BH Paw - Blood, The Journal of the …, 2010 - ashpublications.org
In erythroid cells, ferrous iron is imported into the mitochondrion by mitoferrin-1 (Mfrn1).
Previously, we showed that Mfrn1 interacts with Abcb10 to enhance mitochondrial iron …
Previously, we showed that Mfrn1 interacts with Abcb10 to enhance mitochondrial iron …
Noncanonical coproporphyrin-dependent bacterial heme biosynthesis pathway that does not use protoporphyrin
It has been generally accepted that biosynthesis of protoheme (heme) uses a common set
of core metabolic intermediates that includes protoporphyrin. Herein, we show that the …
of core metabolic intermediates that includes protoporphyrin. Herein, we show that the …
Erythroid heme biosynthesis and its disorders
HA Dailey, PN Meissner - Cold Spring …, 2013 - perspectivesinmedicine.cshlp.org
Heme, which is composed of iron and the small organic molecule protoporphyrin, is an essential
component of hemoglobin as well as a variety of physiologically important hemoproteins…
component of hemoglobin as well as a variety of physiologically important hemoproteins…
[HTML][HTML] Identification of the mitochondrial heme metabolism complex
Heme is an essential cofactor for most organisms and all metazoans. While the individual
enzymes involved in synthesis and utilization of heme are fairly well known, less is known …
enzymes involved in synthesis and utilization of heme are fairly well known, less is known …
Differential interaction of porphyrins used in photoradiation therapy with ferrochelatase
HA Dailey, A Smith - Biochemical Journal, 1984 - portlandpress.com
The mechanism of porphyrin accumulation by tumours is not yet established. If metabolism
aids porphyrin elimination, tumours, unlike normal tissues, may not metabolize porphyrins …
aids porphyrin elimination, tumours, unlike normal tissues, may not metabolize porphyrins …