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Topic: Ferryl

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Hemoglobin

Heme

Hemoprotein

Oxidation

Cytochrome C

	FERRYL 202, FERRYL 103, FERRYL 202 Aluminium, FERRYL 101, FERRYCID, ELECTROCLEAN, FERRYL404 R, FERRYL 401, RUSTOIL, ...
		FERRYL 202Aluminium is for cases where extreme high temperatures can occur, for instance on tankers on hot cover screws where the grease will stand up to a temperature 110° C (230° F) before melting.
		FERRYL 101 is with advantage used for rust protection and lubrication of wires, derricks, running rigging, winches, windlasses, tension wires, lifeboat falls, tank-cover screws, valves, gear-wheels, hatch-cover wheels, bolts, nuts, spindles, etc. or where an oil is preferred to a grease.
		FERRYL 401 is developed for rust protection of bright handrails, nuts, ventilators, binnacles, signs and wherever a completely dry, hard and transparent film is wanted for rust protection and for reducing cleaning.
	www.aeromarineindia.com /products/ferryl.htm (448 words)

	Transition path sampling
		146] In a second step (see last column in table 7.2), the ferryl ion was formed by donation of a proton by one of the hydroxo ligands to the solvent.
		H hydrogen to form the ferryl ion in one step (direct mechanism).
		Formation of the ferryl ion by H-donation of one of the dihydroxo ligands to the solvent is only favorable if the system finds itself on the left-hand-side of equation 7.4.
	www.cmm.upenn.edu /~ensing/thesis/node57.html (1386 words)

	[No title]
		Furthermore, the decay of the heme ferryl compound I to compound II was independent of the proximal HisF8 trans-ligand strength.
		The hydrogen-bonding strength between the TyrB10 and the heme ferryl species suggests the presence of a cycle where the ferryl consumption by the ferric heme increases significantly the pseudoperoxidase activity of these hemeproteins.
		This ferryl mode indicates the absence of hydrogen bonding between the carbonyl group of the distal Q64 and the HbIFe(IV)=O ferryl moiety.
	lib.bioinfo.pl /auth:Cerda,J (2856 words)

	Acellular hemoglobin-mediated oxidative stress toward endothelium: a role for ferryl iron -- Goldman et al. 275 (3): ...
		Acellular hemoglobin-mediated oxidative stress toward endothelium: a role for ferryl iron -- Goldman et al.
		Reactions of human hemoglobin Ao and two cross-linked derivatives with hydrogen peroxide: differential behavior of the ferryl intermediate.
		The globin-based free radical of ferryl hemoglobin is detected in normal human blood.
	ajpheart.physiology.org /cgi/content/full/275/3/H1046 (4092 words)

	[No title] (Site not responding. Last check: 2007-09-10)
		Two of these (suggested to be "peroxy" and "ferryl" species) ale also produced in the reaction of the oxidized enzyme with hydrogen peroxide.
		The same "ferryl" species has also been reported to be produced when two-electron reduced cytochrome bo3 reacts with oxygen, whereas this reaction leads to the "peroxy" intermediate in the cytochrome c oxidases.
		We conclude that the oxygen reaction is similar in the cytochrome c and quinol oxidases.
	www.bioc.rice.edu /~graham/abstracts/abstract9.html (220 words)

	Baby Name Ferryl - Origin and Meaning of Ferryl
		The boy's name Ferryl is a variant of Farrell.
		Similar baby name suggestions for Ferryl are Ferrill, Ferrell, Ferrel, Farryll, Farrel and Veryl.
		Ferryl is a very rare male first name and a very rare surname, according to the 1990 U.S. Census.
	www.thinkbabynames.com /name/1/Ferryl (94 words)

	Methane oxidation by the ferryl ion
		Previously, we have shown that the ferryl ion ([Fe) is easily produced from Fenton's reagent (i.e.
		In order to definitely conclude that the ferryl ion is indeed the active species in oxidation reactions with Fenton's reagent, we have in the present study studied the reactivity of the ferryl ion towards organic substrates, in particular the oxidation of methane to methanol.
		Nevertheless, in combination with our previous work, we must conclude that the ferryl ion is indeed the active intermediate in Fenton chemistry.
	www.cmm.upenn.edu /~ensing/thesis/node61.html (222 words)

	Cytochrome c Oxidase
		The other path is the pathway in which a ferryl state is formed.
		The formation of a ferryl state would require the reduction of four electrons.
		Water is then released when the classical ferryl intermediate is formed.
	www.uvm.edu /~swgordon/131-00/131-webproj/mbarb/reaction.html (780 words)

	Reactions of Sperm Whale Myoglobin with Hydrogen Peroxide. EFFECTS OF DISTAL POCKET MUTATIONS ON THE FORMATION AND ... (Site not responding. Last check: 2007-09-10)
		to ferryl-Mb, 2) autoreduction of the ferryl intermediate to ferric
		The oxidation of myoglobin occurs immediately, as evidenced by the loss of absorption at the 577- and 541-nm bands that are typical of oxyferrous myoglobin, yielding a final spectrum of ferrimyoglobin with characteristic absorportion peaks at 510, 550, and 630 nm.
		The disappearance of oxymyoglobin occurred through the formation of a ferryl intermediate as can be seen by the appearance of the spectrum with peaks at 545 and 580 nm.
	www.jbc.org /cgi/content/full/274/4/2029 (6026 words)

	Understanding the Role of Thiolate Ligation in Nature's Hydroxylating Heme Enzymes
		This energy is determined by the reduction potential of compound I and the pKa of the ferryl species, as in Eq.
		This equation and Green's EXAFS results suggest a novel role for thiolate-ligation in cytochromes P450, namely, that Nature may be using the basic ferryl species afforded by thiolate-ligation to lower the redox potential necessary for hydrogen abstraction (and subsequent hydroxylation) to occur.
		B) The Rebound Intermediate; This figure illustrates that (except for the presence of the hydrocarbon radical) the P450 rebound intermediate and the protonated ferryl of CPO are equivalent.
	www-ssrl.slac.stanford.edu /research/highlights_archive/p450.html (604 words)

	Cruz, A (Anthony)
		This suggests the possible existence of a conformational equilibrium between an open and closed configuration due to the interactions of the TyrB10, ligand, and heme iron.
		The kinetic behavior for the reaction of both ferric proteins with H2O2 indicates that the rate for the formation of the ferryl intermediates species varies with pH, suggesting that the reaction is strongly dependent on the conformational states.
		Moreover, the presence of the A3 and A(o) conformers at 1924 and 1964 cm(-1) in the HbII-CO infrared spectra confirms the existence of an open and closed conformation due to the orientation of the TyrB10 with respect to the heme active center.
	kitphati.lib.bioinfo.pl /auid:5005905 (684 words)

	Amazon.com: "ferryl oxygen atom": Key Phrase page (Site not responding. Last check: 2007-09-10)
		From this work, based mainly upon reactions of substituted hydrazines, the ferryl oxygen atom and most of the heme of HRP-I are believed to be inaccessible to reducing substrate.
		the ferryl oxygen atom as water, do not come from the substrate but are most likely obtained from the bulk water solution:...
		The intermediacy of ferryl species in these reactions could not however be eliminated if the ferryl oxygen atom arose from the labelled H202.
	www.amazon.com /phrase/ferryl-oxygen-atom (534 words)

	Interactions of hemoglobin with hydrogen peroxide alters thiol levels and course of endothelial cell death -- D'Agnillo ...
		of oxy (Fe), met (Fe), and ferryl (Fe) forms of Hb were calculated as previously described (12, 64).
		of the ferryl intermediate, as evidenced by the appearance of
		In this study, we further explored the contribution of cell-free Hb to cell injury and death.
	ajpheart.physiology.org /cgi/content/full/279/4/H1880 (5418 words)

	Dalton Transactions Articles
		(ferryl and porphyrin cation radical) types and which may precede the formation of ferrylmyoglobin.
		To test the hypothesis that the distal histidine facilitates ferryl formation we studied the myoglobin-like haemoglobin from the gastropod mollusc Aplysia fasciata, where this histidine is replaced by valine and its hydrogen bonding role is taken up by a non-homologous arginine.
		Thirdly, as ferryl haems and associated free radicals may play a role in disease, we have studied the action of myoglobin—peroxide mixtures towards external reductants.
	www.rsc.org /Publishing/Journals/DT/article.asp?doi=b505786h (309 words)

	Hemoglobin Toxicity in Experimental Bacterial Peritonitis Is Due to Production of Reactive Oxygen Species -- Yoo et al. ...
		OH and/or ferryl ion [Fe(IV)==O] in the presence of H
		OH or ferryl ion in the presence of Fenton reagents.
		OH and ferryl ion are highly reactive species and react with a variety of biological molecules such as protein, membrane lipid,
	cdli.asm.org /cgi/content/full/6/6/938 (3949 words)

	[No title] (Site not responding. Last check: 2007-09-10)
		These "ferryl" species in the past have proven difficult to characterize because of their high reactivity.
		A novel and powerful method to generate and detect them will be developed that depends first on using methods of molecular biology to engineer the proteins so as to facilitate electron transfer reactions that can be driven by a short flash of laser light.
		The ferryl species will then be detected by use of their optical properties, and information on their reactivity will be obtained directly.
	www.cs.utexas.edu /users/yguan/NSFAbstracts/Abstracts/MPS/CHE.MPS.a9214569.txt (265 words)

	Detection of ferryl myoglobin in the isolated ischemic rat heart. (Site not responding. Last check: 2007-09-10)
		Detection of ferryl myoglobin in the isolated ischemic rat heart.
		Reflectance spectroscopy was utilized to monitor the oxidation states of myoglobin (Mb) in isolated, buffer-perfused rat hearts.
		The addition of Na2S to the buffer at reperfusion permitted the detection of ferryl myoglobin (MbIV) as its sulfmyoglobin derivative.
	www.galenicom.com /medline/article/2079231/au:Eddy+L (207 words)

	APStracts 5:0246H, 1998. (Site not responding. Last check: 2007-09-10)
		However, reaction of the modified hemoglobins, but not HbA0, with hydrogen peroxide induced apoptotic cell death (as assessed by morphologic changes and DNA fragmentation) that correlated with the formation of a long-lived ferrylhemoglobin.
		A preparation of ferryl a-DBBF free of residual peroxide rapidly induced morphologic changes and DNA fragmentation in BAEC indicative of apoptotic cell death.
		Redox cycling of chemically modified hemoglobins by peroxide yielded a persistent ferryl iron which was cytotoxic to endothelial cells.
	www.uth.tmc.edu /apstracts/1998/heart/July/246H.html (233 words)

	C&EN: LATEST NEWS - PUTTING THE OH WHERE IT BELONGS
		This highly reactive ferryl radical species is thought to abstract hydrogen from the hydrocarbon substrate, forming a protonated ferryl that then hydroxylates the substrate.
		His early studies of synthetic model systems indicate that the reactivity of ferryl species depends on both their redox potential and the ease with which their reduced forms can be protonated.
		So because the electron-donating thiolate linkage makes it easier to protonate the ferryl species, P450s can rely on ferryl radicals whose redox potentials are lower than what would normally be required to hydroxylate inert hydrocarbon substrates, Green says.
	pubs.acs.org /cen/news/8224/8224notw6.html (487 words)

	Department of Chemistry
		The intermediates of peroxidase and catalase are typified by two highly oxidizing enzymatic states known as compounds I and II, which respectively are two and one oxidizing equivalents above the resting enzyme.
		Compound II contains the heme iron in the Fe(IV) state (ferryl), while compound I contains the ferryl heme with an additional electron removed from the porphyrin ring.
		Though our major findings have arisen from studies of the ferryl type intermediates (compound II of horseradish peroxidase and lactoperoxidase, compound ES of cytochrome c peroxidase, etc.) we have recently been able to resolve resonance Raman signals from the elusive compound I intermediates of horseradish peroxidase and chloroperoxidase.
	www.has.vcu.edu /che/people/bio/terner.html (610 words)

	The Globin-based Free Radical of Ferryl Hemoglobin Is Detected in Normal Human Blood -- Svistunenko et al. 272 (11): ... (Site not responding. Last check: 2007-09-10)
		The Globin-based Free Radical of Ferryl Hemoglobin Is Detected in Normal Human Blood -- Svistunenko et al.
		The reaction between heme proteins and peroxides is known to proceed via formation of two intermediates, a ferryl heme iron,
		In fact, formation of a ferryl form of the heme protein was demonstrated
	www.jbc.org /cgi/content/full/272/11/7114 (6074 words)

	Molecular Modeling of Human P450c17 (17{alpha}-Hydroxylase/ 17,20-Lyase): Insights into Reaction Mechanisms and Effects ...
		The heme group is shown in red; the ferryl oxygen is green; the hydroxyl of T306 is orange; hydrophobic residues of P450c17 are shown in gray while hydrophilic residues are shown in cyan.
		that led to the ferryl peroxide proposal (50).
		The ferryl oxene permits hydrogen abstraction at the C17 hydroxyl of 17-OH-pregnenolone (I) to generate a hydroxyl radical (II) that fragments into DHEA (III) and an acetyl radical (IV).
	mend.endojournals.org /cgi/content/full/13/7/1169 (7418 words)

	Abstract 33 (Site not responding. Last check: 2007-09-10)
		The peroxy species decay to a ferryl intermediate, with a peak at 578 nm versus the oxidized enzyme, following by electron redistribution between Cu and cytochrome a.
		The two ferryl species reach a maximum concentration ~310 us after photolysis.
		The excellent agreement between the experimental and theoretical spectra of the intermediates provides unequivocal evidence for the presence of peroxy and ferryl species during dioxygen reduction by cytochrome oxidase at room temperature.
	www.bioc.rice.edu /~graham/abstracts/abstract33.html (272 words)

	Redox cycling of diaspirin cross-linked hemoglobin induces G2/M arrest and apoptosis in cultured endothelial cells -- ...
		Ferryl hemoglobin was measured using the sodium sulfide method as described in "Materials and methods." Each point represents the mean ± SE for 4 to 5 samples.
		Figure 1B shows the time-dependent fractional changes in the ferrous, ferryl, and ferric states after the addition of GOX
		The fraction of cells in the (A) G1 phase, (B) S phase, and (C) G2/M phase of the cell cycle was calculated as described in "Materials and methods." Each point represents the mean ± SE for 3 to 6 independent experiments.
	www.bloodjournal.org /cgi/content/full/98/12/3315 (6166 words)

	Marian Fabian \| Department of Biochemistry \| Rice University
		Fabian, M., and Palmer, G. "Proton involvement in the transition of "peroxy" to "ferryl" intermediate of cytochrome c oxidase." Biochemistry, 40 (2001): 1867-1874.
		Fabian, M., and Palmer, G. "Proton Involvement in Transition of "Peroxy" to "Ferryl" Intermediate of Cytochrome c Oxidase." Biochim.
		Fabian, M., and Palmer, G. "The Redox State of Peroxy and Ferryl Intermediates in Cytochrome c Oxidase Catalysis." Biochemistry, 38 (1999): 6270-6275.
	biochem.rice.edu /facultydetail_new.cfm?riceid=1025 (475 words)

	Introduction
		197] Our studies show that the ferryl ion is easily formed from hydrogen peroxide coordinated to pentaaqua iron(II), and from the energetic point of view much more likely than the formation of free OH.
		However, to definitively accept the ferryl ion as the active species in aqueous Fenton chemistry, we need to investigate whether the ferryl ion is indeed capable of oxidizing organic substrates.
		To investigate the solvent effects on oxidation chemistry by the ferryl ion, we have also computed the free energy profile for the methane hydroxylation by the ferryl ion (according to the oxygen-rebound mechanism) in aqueous solution, using constrained ab initio molecular dynamics (section 8.4).
	www.cmm.upenn.edu /~ensing/thesis/node62.html (919 words)

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