Format
Sort by
Items per page

Send to

Choose Destination

Search results

Items: 1 to 50 of 133

1.
2.

Multiple exo-glycosidases in human serum as detected with the substrate DNP-α-GalNAc. I. A new assay for lysosomal α-N-acetylgalactosaminidase.

Albracht SPJ, Allon E, van Pelt J.

BBA Clin. 2017 Oct 7;8:84-89. doi: 10.1016/j.bbacli.2017.10.001. eCollection 2017 Dec.

3.
4.

The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited: II. Comparison of the proposed working hypothesis with literature data.

Albracht SP.

J Bioenerg Biomembr. 2010 Aug;42(4):279-92. doi: 10.1007/s10863-010-9302-y. Epub 2010 Jul 15.

PMID:
20632077
5.

The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited: I. Proposed consequences for electron transfer in the enzyme.

Albracht SP.

J Bioenerg Biomembr. 2010 Aug;42(4):261-78. doi: 10.1007/s10863-010-9301-z. Epub 2010 Jul 14.

PMID:
20628895
6.

Toward single-enzyme molecule electrochemistry: [NiFe]-hydrogenase protein film voltammetry at nanoelectrodes.

Hoeben FJ, Meijer FS, Dekker C, Albracht SP, Heering HA, Lemay SG.

ACS Nano. 2008 Dec 23;2(12):2497-504. doi: 10.1021/nn800518d.

PMID:
19206284
7.

Spin distribution of the H-cluster in the H(ox)-CO state of the [FeFe] hydrogenase from Desulfovibrio desulfuricans: HYSCORE and ENDOR study of (14)N and (13)C nuclear interactions.

Silakov A, Wenk B, Reijerse E, Albracht SP, Lubitz W.

J Biol Inorg Chem. 2009 Feb;14(2):301-13. doi: 10.1007/s00775-008-0449-5. Epub 2008 Nov 15.

PMID:
19011912
8.

Polymyxin-coated Au and carbon nanotube electrodes for stable [NiFe]-hydrogenase film voltammetry.

Hoeben FJ, Heller I, Albracht SP, Dekker C, Lemay SG, Heering HA.

Langmuir. 2008 Jun 3;24(11):5925-31. doi: 10.1021/la703984z. Epub 2008 May 7.

PMID:
18459755
9.

The electronic structure of the H-cluster in the [FeFe]-hydrogenase from Desulfovibrio desulfuricans: a Q-band 57Fe-ENDOR and HYSCORE study.

Silakov A, Reijerse EJ, Albracht SP, Hatchikian EC, Lubitz W.

J Am Chem Soc. 2007 Sep 19;129(37):11447-58. Epub 2007 Aug 28.

PMID:
17722921
10.

Characterization of a cyanobacterial-like uptake [NiFe] hydrogenase: EPR and FTIR spectroscopic studies of the enzyme from Acidithiobacillus ferrooxidans.

Schröder O, Bleijlevens B, de Jongh TE, Chen Z, Li T, Fischer J, Förster J, Friedrich CG, Bagley KA, Albracht SP, Lubitz W.

J Biol Inorg Chem. 2007 Feb;12(2):212-33. Epub 2006 Nov 3.

PMID:
17082918
11.

Characterization of a HoxEFUYH type of [NiFe] hydrogenase from Allochromatium vinosum and some EPR and IR properties of the hydrogenase module.

Long M, Liu J, Chen Z, Bleijlevens B, Roseboom W, Albracht SP.

J Biol Inorg Chem. 2007 Jan;12(1):62-78. Epub 2006 Sep 13.

PMID:
16969669
12.

[NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation.

Burgdorf T, Lenz O, Buhrke T, van der Linden E, Jones AK, Albracht SP, Friedrich B.

J Mol Microbiol Biotechnol. 2005;10(2-4):181-96. Review.

PMID:
16645314
13.

An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: new insights into its (in)stability and spectroscopic properties.

van der Linden E, Burgdorf T, de Lacey AL, Buhrke T, Scholte M, Fernandez VM, Friedrich B, Albracht SP.

J Biol Inorg Chem. 2006 Mar;11(2):247-60. Epub 2006 Jan 18.

PMID:
16418856
14.

Electrochemical definitions of O2 sensitivity and oxidative inactivation in hydrogenases.

Vincent KA, Parkin A, Lenz O, Albracht SP, Fontecilla-Camps JC, Cammack R, Friedrich B, Armstrong FA.

J Am Chem Soc. 2005 Dec 28;127(51):18179-89.

PMID:
16366571
15.
16.

The active site of the [FeFe]-hydrogenase from Desulfovibrio desulfuricans. II. Redox properties, light sensitivity and CO-ligand exchange as observed by infrared spectroscopy.

Roseboom W, De Lacey AL, Fernandez VM, Hatchikian EC, Albracht SP.

J Biol Inorg Chem. 2006 Jan;11(1):102-18. Epub 2005 Dec 2.

PMID:
16323019
17.

Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases.

Volbeda A, Martin L, Cavazza C, Matho M, Faber BW, Roseboom W, Albracht SP, Garcin E, Rousset M, Fontecilla-Camps JC.

J Biol Inorg Chem. 2005 Aug;10(5):591. doi: 10.1007/s00775-005-0663-3. No abstract available.

PMID:
27518782
18.

[NiFe]-hydrogenases: spectroscopic and electrochemical definition of reactions and intermediates.

Armstrong FA, Albracht SP.

Philos Trans A Math Phys Eng Sci. 2005 Apr 15;363(1829):937-54; discussion 1035-40. Review.

PMID:
15991402
19.

The mechanism of activation of a [NiFe]-hydrogenase by electrons, hydrogen, and carbon monoxide.

Lamle SE, Albracht SP, Armstrong FA.

J Am Chem Soc. 2005 May 11;127(18):6595-604.

PMID:
15869280
20.

The soluble NAD+-Reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH.

Burgdorf T, van der Linden E, Bernhard M, Yin QY, Back JW, Hartog AF, Muijsers AO, de Koster CG, Albracht SP, Friedrich B.

J Bacteriol. 2005 May;187(9):3122-32.

21.

Structural differences between the ready and unready oxidized states of [NiFe] hydrogenases.

Volbeda A, Martin L, Cavazza C, Matho M, Faber BW, Roseboom W, Albracht SP, Garcin E, Rousset M, Fontecilla-Camps JC.

J Biol Inorg Chem. 2005 May;10(3):239-49. Epub 2005 Apr 1. Erratum in: J Biol Inorg Chem. 2005 Aug;10(5):591. J Biol Inorg Chem. 2005 Aug;10(5):591.

PMID:
15803334
22.

Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopy.

Burgdorf T, Löscher S, Liebisch P, Van der Linden E, Galander M, Lendzian F, Meyer-Klaucke W, Albracht SP, Friedrich B, Dau H, Haumann M.

J Am Chem Soc. 2005 Jan 19;127(2):576-92.

PMID:
15643882
23.

The biosynthetic routes for carbon monoxide and cyanide in the Ni-Fe active site of hydrogenases are different.

Roseboom W, Blokesch M, Böck A, Albracht SP.

FEBS Lett. 2005 Jan 17;579(2):469-72.

25.
26.

The complex between hydrogenase-maturation proteins HypC and HypD is an intermediate in the supply of cyanide to the active site iron of [NiFe]-hydrogenases.

Blokesch M, Albracht SP, Matzanke BF, Drapal NM, Jacobi A, Böck A.

J Mol Biol. 2004 Nov 12;344(1):155-67.

PMID:
15504408
27.

The auxiliary protein HypX provides oxygen tolerance to the soluble [NiFe]-hydrogenase of ralstonia eutropha H16 by way of a cyanide ligand to nickel.

Bleijlevens B, Buhrke T, van der Linden E, Friedrich B, Albracht SP.

J Biol Chem. 2004 Nov 5;279(45):46686-91. Epub 2004 Aug 31.

28.

The activation of the [NiFe]-hydrogenase from Allochromatium vinosum. An infrared spectro-electrochemical study.

Bleijlevens B, van Broekhuizen FA, De Lacey AL, Roseboom W, Fernandez VM, Albracht SP.

J Biol Inorg Chem. 2004 Sep;9(6):743-52. Epub 2004 Jul 9.

PMID:
15243788
29.

The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen.

Van der Linden E, Burgdorf T, Bernhard M, Bleijlevens B, Friedrich B, Albracht SP.

J Biol Inorg Chem. 2004 Jul;9(5):616-26. Epub 2004 May 26.

PMID:
15164270
30.

Hydrogen-induced activation of the [NiFe]-hydrogenase from Allochromatium vinosum as studied by stopped-flow infrared spectroscopy.

Kurkin S, George SJ, Thorneley RN, Albracht SP.

Biochemistry. 2004 Jun 1;43(21):6820-31.

PMID:
15157116
31.

Reactions of H2, CO, and O2 with active [NiFe]-hydrogenase from Allochromatium vinosum. A stopped-flow infrared study.

George SJ, Kurkin S, Thorneley RN, Albracht SP.

Biochemistry. 2004 Jun 1;43(21):6808-19.

PMID:
15157115
32.

Selective release and function of one of the two FMN groups in the cytoplasmic NAD+-reducing [NiFe]-hydrogenase from Ralstonia eutropha.

van der Linden E, Faber BW, Bleijlevens B, Burgdorf T, Bernhard M, Friedrich B, Albracht SP.

Eur J Biochem. 2004 Feb;271(4):801-8.

33.

Enzyme electrokinetics: electrochemical studies of the anaerobic interconversions between active and inactive states of Allochromatium vinosum [NiFe]-hydrogenase.

Jones AK, Lamle SE, Pershad HR, Vincent KA, Albracht SP, Armstrong FA.

J Am Chem Soc. 2003 Jul 16;125(28):8505-14.

PMID:
12848556
34.

Two EPR-detectable [4Fe-4S] clusters, N2a and N2b, are bound to the NuoI (TYKY) subunit of NADH:ubiquinone oxidoreductase (Complex I) from Rhodobacter capsulatus.

Chevallet M, Dupuis A, Issartel JP, Lunardi J, van Belzen R, Albracht SP.

Biochim Biophys Acta. 2003 Mar 6;1557(1-3):51-66.

35.
36.

Enzyme electrokinetics: hydrogen evolution and oxidation by Allochromatium vinosum [NiFe]-hydrogenase.

Léger C, Jones AK, Roseboom W, Albracht SP, Armstrong FA.

Biochemistry. 2002 Dec 31;41(52):15736-46.

PMID:
12501202
37.

The membrane-bound [NiFe]-hydrogenase (Ech) from Methanosarcina barkeri: unusual properties of the iron-sulphur clusters.

Kurkin S, Meuer J, Koch J, Hedderich R, Albracht SP.

Eur J Biochem. 2002 Dec;269(24):6101-11.

38.

Direct comparison of the electrocatalytic oxidation of hydrogen by an enzyme and a platinum catalyst.

Jones AK, Sillery E, Albracht SP, Armstrong FA.

Chem Commun (Camb). 2002 Apr 21;(8):866-7.

PMID:
12123018
39.

Involvement of hyp gene products in maturation of the H(2)-sensing [NiFe] hydrogenase of Ralstonia eutropha.

Buhrke T, Bleijlevens B, Albracht SP, Friedrich B.

J Bacteriol. 2001 Dec;183(24):7087-93.

41.

A paramagnetic species with unique EPR characteristics in the active site of heterodisulfide reductase from methanogenic archaea.

Madadi-Kahkesh S, Duin EC, Heim S, Albracht SP, Johnson MK, Hedderich R.

Eur J Biochem. 2001 May;268(9):2566-77.

42.

The H2 sensor of Ralstonia eutropha. Biochemical characteristics, spectroscopic properties, and its interaction with a histidine protein kinase.

Bernhard M, Buhrke T, Bleijlevens B, De Lacey AL, Fernandez VM, Albracht SP, Friedrich B.

J Biol Chem. 2001 May 11;276(19):15592-7. Epub 2001 Feb 16.

43.

A stable organic free radical in anaerobic benzylsuccinate synthase of Azoarcus sp. strain T.

Krieger CJ, Roseboom W, Albracht SP, Spormann AM.

J Biol Chem. 2001 Apr 20;276(16):12924-7. Epub 2001 Jan 30.

44.
45.

Structural examination of the nickel site in chromatium vinosum hydrogenase: redox state oscillations and structural changes accompanying reductive activation and CO binding.

Davidson G, Choudhury SB, Gu Z, Bose K, Roseboom W, Albracht SP, Maroney MJ.

Biochemistry. 2000 Jun 27;39(25):7468-79.

PMID:
10858296
46.

Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha.

Happe RP, Roseboom W, Egert G, Friedrich CG, Massanz C, Friedrich B, Albracht SP.

FEBS Lett. 2000 Jan 28;466(2-3):259-63.

47.

Orientation-selected ENDOR of the active center in Chromatium vinosum [NiFe] hydrogenase in the oxidized "ready" state.

Gessner C, Stein M, Albracht SP, Lubitz W.

J Biol Inorg Chem. 1999 Aug;4(4):379-89.

PMID:
10555572
49.
50.

Supplemental Content

Loading ...
Support Center