Carotenoid incorporation into microsomes: yields, stability and membrane dynamics

Socaciu, Carmen; Jessel, Robert; Diehl, H.

doi:10.1016/s1386-1425(00)00375-9

Cited by 28 publications

(21 citation statements)

References 21 publications

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“…2). Also, substrates for CCOs are highly lipophilic and tend to reside in hydrophobic environments, such as plant thylakoid membranes (10) or liposomes in mammals (11)(12)(13). Accordingly, CCOs show varying levels of membrane association, from soluble to integral (14)(15)(16).…”

Section: Resultsmentioning

confidence: 99%

Structure and mechanism of NOV1, a resveratrol-cleaving dioxygenase

McAndrew

Sathitsuksanoh

Mbughuni

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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Stilbenes are diphenyl ethene compounds produced naturally in a wide variety of plant species and some bacteria. Stilbenes are also derived from lignin during kraft pulping. Stilbene cleavage oxygenases (SCOs) cleave the central double bond of stilbenes, forming two phenolic aldehydes. Here, we report the structure of an SCO. The X-ray structure of NOV1 from Novosphingobium aromaticivorans was determined in complex with its substrate resveratrol (1.89 Å), its product vanillin (1.75 Å), and without any bound ligand (1.61 Å). The enzyme is a seven-bladed β-propeller with an iron cofactor coordinated by four histidines. In all three structures, dioxygen is observed bound to the iron in a side-on fashion. These structures, along with EPR analysis, allow us to propose a mechanism in which a ferric-superoxide reacts with substrate activated by deprotonation of a phenol group at position 4 of the substrate, which allows movement of electron density toward the central double bond and thus facilitates reaction with the ferric superoxide electrophile. Correspondingly, NOV1 cleaves a wide range of other stilbene-like compounds with a 4′-OH group, offering potential in processing some solubilized fragments of lignin into monomer aromatic compounds.tilbenes are diphenyl ethene compounds that are produced naturally in a wide variety of plant species and some bacteria. One stilbene derivative of note is resveratrol, which is a plant phytoalexin abundant in grapes and peanuts. Studies have demonstrated numerous health benefits related to the consumption of resveratrol, which is correlated with reduced cardiovascular disease and cancer (1). Lignostilbene α,β-dioxygenase (LSD, EC 1.13.11.43), originally observed in Sphingomonas paucimobilis, was the first enzyme shown to cleave the central double bond of stilbenes, forming two phenolic aldehydes (2, 3). Subsequently, NOV1 and NOV2 (4) from Novosphingobium aromaticivorans, Rco1 (5) from Ustilago maydis, and CAO-1 (6) from Neurospora crassa were also shown to be stilbene cleaving oxygenases (SCOs). SCOs are related to carotenoid cleavage oxygenases (CCOs), which are enzymes that oxidatively cleave β-carotene or apocarotenoids. Carotenoids are a diverse class of molecules that play important roles in photosynthesis, immune function, and light perception in the eye. CCOs have been studied in great detail, including several crystal structures (7-9).Here, we present the X-ray structure of an SCO, NOV1 from N. aromaticivorans (NOV1). The structure was determined in complex with a representative substrate (resveratrol), a representative product (vanillin), and without ligand bound. We have also observed the ternary complex with oxygen and substrate or product bound, which has not been previously detected in a crystal structure of any CCO-related enzyme. Despite being related to CCOs, this structure of NOV1 shows several key differences that are indicative of their disparate substrate specificities. Moreover, the observed placement of Fe, O 2 , and the phenolic substrate resveratrol in th...

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Section: Resultsmentioning

confidence: 99%

Structure and mechanism of NOV1, a resveratrol-cleaving dioxygenase

McAndrew

Sathitsuksanoh

Mbughuni

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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“…After centrifuging at 22,500g at 0°C for 15 min, the free Ax and supernatant were removed and Ax-colored microsomes were resuspended in 360 µL of 0.1 M potassium phosphate buffer (pH 7.4). According to previous report, approximately 10 % of Ax is incorporated into microsomal membrane [Socaciu et al, 2000]. Therefore, Ax incorporated samples were considered to contain Ax from 0.0002 -0.2 mM.…”

Section: Incorporation Of Ax To Liver Microsomesmentioning

confidence: 99%

Astaxanthin can alter CYP1A-dependent activities via two different mechanisms: Induction of protein expression and inhibition of NADPH P450 reductase dependent electron transfer

Ohno

Darwish

Ikenaka

et al. 2011

Food and Chemical Toxicology

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1A-dependent activity. CYP1A is one of the most important enzymes participating in phase I metabolism for chemicals, and it can activate various mutagens. To investigate the effect of Ax on the metabolic activation of a typical promutagen, benzo[a]pyrene by CYP1A, we orally administrated Ax (100 mg / kg body weight / day for 3 days) to male Wistar rats. In the treated rat liver, expression of CYP1A1 mRNA, protein, and its activity were significantly increased (5.5-fold, 8.5-fold, and 2.5-fold, respectively). In contrast, the activities of phase II enzymes (glutathione S-transferase and glucuronosyl-transferase)were not modulated by Ax. As a consequence, the mutagenicity of benzo[a]pyrene was more enhanced in Ax-treated rats, compared with controls in the Ames assay. On the other hand, NADPH P450 reductase activity was decreased in liver microsomes from the treated group. This result suggests the possibility that Ax inhibits the electron supply necessary for CYP catalytic activities and decreases CYP1A activity indirectly. In conclusion, Ax intake can alter CYP1A-dependent activities through two different mechanisms: 1) induction of CYP1A1 mRNA, protein expression, and activity; and 2) inhibition of the electron supply for the enzyme.

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“…In nat u ral and model mem branes, zeaxanthin appears to have the stron gest in flu ence on such membrane prop er ties as tem per a ture of phase tran si tion, mo lec u lar dy nam ics, per me abil ity and po lar ity gradi ent (Lazrak et al 1987, Gruszecki and Strzałka 1991, Subczyński et al 1991, Subczyński et al 1992, Havaux and Gruszecki 1993, Tardy et al 1997, Jagannadham et al 2000, Socaciu et al 2000, Kostecka-Gugała et al 2003. It was shown for two ant arc tic bac te rial spe cies, Sphingobacterium antarcticus and Sphingo bacterium multivorum, that mem brane flu id ity is reg u lated mainly by Zx (Jagannadham et al 2000).…”

Section: Reg U La Tion Of Mem Brane Phys I Cal Prop Er Tiesmentioning

confidence: 99%

The xanthophyll cycle - molecular mechanism and physiological significance

2004

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2 De part ment of Chem is try, Ped a gog i cal Uni ver sity, ul. Podchorążych 2, 30-084 Kraków, Po land Key words: antheraxanthin; lipocalin; mem brane prop er ties; mo lec u lar mech a nism; photopro tection; sig nif i cance; the xanthophyll cy cle; violaxanthin; violaxanthin de-epoxidase; zeaxanthin; zeaxanthin epoxidase Ab stractThe light-dependent, cy clic changes of xanthophyll pig ments: violaxanthin, antheraxanthin and zeaxanthin, called the xantho phyll cy cle, have been known for about fifty years. This pro cess was char ac ter ised for higher plants, sev eral fern and moss spe cies and in some al gal groups. Two en zymes, violaxanthin de-epoxidase (VDE) and zeaxanthin epoxidase (ZE), be long ing to the lipocalin pro tein fam ily, are en gaged in the xantho phyll cy cle. VDE re quires for its ac tiv ity ascor bic acid and re versed hex ag o nal struc ture formed by monogalactosyl di acylglycerol. ZE, pos tu lated to be a flavoprotein, has not been pu ri fied yet and it is known from its gene se quence only. Zeaxanthin epoxidation is de pend ent on the re duc ing power of NADPH and pres ence of ad di tional proteins.The xanthophyll cy cle is pos tu lated to play a role in many impor tant phys i o log i cal pro cesses. Zeaxanthin, formed from violaxanthin un der high light con di tions, is thought to be a main photoprotector in autotrophic cells due to its abil ity to dis si pate ex cess of ab sorbed light en ergy that can be mea sured as a non-photochemical quench ing. In ad di tion the zeaxanthin for ma tion is im por tant in pro tec tion of the thylakoid membranes against lipid peroxidation. Other pos tu lated func tions of the xanthophyll cy cle, which in clude reg u la tion of membrane phys i cal prop er ties, blue light re cep tion and reg u la tion of abscisic acid syn the sis, are also dis cussed. List of ab bre vi a tions:VDE; violaxanthin de-epoxidase Vx; violaxanthin MGDG; monogalactosyldiacylglycerol DGDG; digalactosyldiacylglycerol PE; phosphatidylethanolamine Zx; zeaxanthin Ax; antheraxanthin Xc; xanthophyll cy cle ZE; zeaxanthin epoxidase NPQ; non-photochemical quench ing ABA; abscisic acid DTT; dithiothreitol SCR; short con ser va tive mo tifs H II ; re versed hex ag o nal struc ture In tro duc tionLight is one of the most im por tant en vi ron men tal fac tors in flu enc ing photosynthetic ac tiv ity of green plants. The ab sorp tion of light by an tenna pig ments and the trans fer of ex ci ta tion en ergy to the re ac tion cen tres of Photosystems I and II are the pri mary steps in this pro cess. To achieve high ef fi ciency of pho to syn the sis, plants have de vel oped reg u la tory mech a nisms to adapt their photosynthetic ap pa ratus to vari able light con di tions, which can rap idly

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Carotenoid incorporation into microsomes: yields, stability and membrane dynamics

Cited by 28 publications

References 21 publications

Structure and mechanism of NOV1, a resveratrol-cleaving dioxygenase

Structure and mechanism of NOV1, a resveratrol-cleaving dioxygenase

Astaxanthin can alter CYP1A-dependent activities via two different mechanisms: Induction of protein expression and inhibition of NADPH P450 reductase dependent electron transfer

The xanthophyll cycle - molecular mechanism and physiological significance

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