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Topic: Heme

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Porphyrin

Ferryl

Hemoglobin

Hemoprotein

Porphyria

Cytochrome C

Leukocyte

Iron

Mitochondrion

Histidine

Red blood cell

Catalase

Chlorophyll

Lead poisoning

	Heme Synthesis
		Using isotopic tracers, it was initially found that N and C atoms of heme are derived from glycine and acetate.
		of the heme synthesis pathway, and is usually rate-limiting for the overall pathway.
		Symptoms vary depending on the enzyme, the severity of the deficiency and whether heme synthesis is affected primarily in liver or in developing erythrocytes.
	www.rpi.edu /dept/bcbp/molbiochem/MBWeb/mb2/part1/heme.htm (768 words)

	Heme and Iron (Site not responding. Last check: )
		Heme metabolism is an important metabolic process because many important proteins contain heme as a prosthetic group.
		Heme is a member of a family of compounds called porphyrins.
		Heme synthesis occurs partly in the mitochondria and partly in the cytoplasm.
	library.med.utah.edu /NetBiochem/hi.htm (199 words)

	Johns Hopkins Medicine - Sylvain Doré's heme
		Heme oxygenase: Heme oxygenase is the only enzyme in the body that can degrade heme, and it generates different metabolites with specific actions: iron, biliverdin/bilirubin, and carbon monoxide.
		Heme, or iron protoporphyrin IX, is a prooxidant.
		Heme is not recycled and must be degraded.
	www.hopkinsmedicine.org /dorelab/heme.html (564 words)

	Heme
		The general questions: Heme is found in many different locations including the mitochondrion (respiratory cytochromes), the chloroplast (photosynthetic cytochromes), the endoplasmic reticulum (P450 cytochromes), the nucleus (heme-responsive transcription factors), the cytosol (catalases), the peroxisomes (catalases) and extracellular compartments (peroxidases).
		Heme attachment is a terminal (or near terminal) step in their maturation, occurring on the p-side of the energy transducing membrane where the cytochromes function.
		In collaboration with the Wollman group (Institut de Biologie Physico-Chimique, Paris), we deduced a pathway for the stepwise association of the bL and bH hemes of holocytochrome b6 in vivo (40).
	www.chem.ucla.edu /dept/Faculty/merchant/heme.html (604 words)

	Heme
		A heme is a metal-containing cofactor that consists of an iron atom contained in the center of a large heterocyclic organic ring called a porphyrin.
		Heme b is not covalently bound to the apoprotein[?] it is found in.
		Heme a differs from heme b in that a methyl side chain is oxidized into a formyl group, and one of the vinyl side chains has been replaced by an isoprenoid chain.
	www.ebroadcast.com.au /lookup/encyclopedia/he/Heme.html (230 words)

	News \| TimesDaily.com \| TimesDaily \| Florence, AL (Site not responding. Last check: )
		Generally, heme B is attached to the surrounding protein matrix (known as the apoprotein) through a single coordination bond between the heme iron and an amino acid side-chain.
		Heme A differs from heme B in that a methyl side chain at ring position 8 is oxidized into a formyl group, and one of the vinyl side chains, at ring position 2, has been replaced by an isoprenoid chain.
		Heme L is one important characteristic of animal peroxidases; plant peroxidases incorporate heme B. Lactoperoxidase and eosinophil peroxidase are protective enzymes responsible for the destruction of invading bacteria and virus.
	www.timesdaily.com /apps/pbcs.dll/section?category=NEWS&template=wiki&text=Heme (1371 words)

	Iron, Heme and Porphyrin Metabolism
		There are a number of heme containing proteins involved in the transport of oxygen (hemoglobin), oxygen storage (myoglobin) and enzyme catalysis such as nitric oxide synthase (NOS) and prostaglandin synthase (cyclooxygenase).
		Heme is oxidized, with the heme ring being opened by the endoplasmic reticulum enzyme, heme oxygenase.
		Pathway for the degradation of heme to bilirubin
	web.indstate.edu /thcme/mwking/heme-porphyrin.html (2906 words)

	Heme Deficiency in Neurons Causes Metabolic Disruptions Similar to Alzheimer's Disease - DERT
		Heme deficiency was detrimental to normal mitochondrial function, stimulated oxidative stress by activating nitric oxide synthase, altered amyloid proteins, and inhibited zinc and iron homeostasis.
		In addition, degradation of heme by heme oxygenase, which increases with age and in the brains of Alzheimer's patients, may be a factor in changes in the metabolism of iron and heme with age.
		Heme deficiency may be a factor in the mitochondrial and neuronal decay of aging.
	www.niehs.nih.gov /dert/profiles/hilites/2002/heme.htm (273 words)

	heme
		Analysis of the components of the three c-cytochrome assembly pathways occurring in plastids, mitochondria and bacteria (47) predicts the existence of a specific heme export pathway in Saccharomyces and mammalian mitochondria.
		Yet, heme export from the mitochondrion is a fundamental and important metabolic function.
		We are presently engaged in a gain of function multi-copy suppressor approach for its identification in Saccharomyces, which should open the door to understanding heme flux in a eukaryotic cell.
	www.chem.ucla.edu /dept/Faculty/heme.html (702 words)

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