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Keywords: haem
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Articles
Biochem Soc Trans (2015) 43 (5): 943–951.
Published: 09 October 2015
... of the mitochondria, whereas ABCB10 is involved in haem biosynthesis. They also play a role in preventing oxidative stress. Mutations in ABCB6 and ABCB7 have been linked to human disease. Recent crystal structures of yeast Atm1 and human ABCB10 have been key to identifying substrate-binding sites and transport...
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Biochem Soc Trans (2013) 41 (6): 1588–1592.
Published: 20 November 2013
... our current knowledge of the molecular mechanisms involved in the handling of iron by astrocytes. Cultured astrocytes efficiently take up iron as ferrous or ferric iron ions or as haem by specific iron transport proteins in their cell membrane. In addition, astrocytes accumulate large amounts of iron...
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Biochem Soc Trans (2012) 40 (6): 1268–1273.
Published: 21 November 2012
... length. In the present paper, DmsE is further characterized via protein film voltammetry, revealing that the electrochemistry of the DmsE haem cofactors display macroscopic potentials lower than those of MtrA by 100 mV. It is possible this tuning of the redox potential of DmsE is required to shuttle...
Includes: Supplementary data
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Biochem Soc Trans (2012) 40 (6): 1217–1221.
Published: 21 November 2012
.... This serves to highlight several unanswered questions relating to the regulation of respiratory electron transport in Shewanella and the central role(s) of the tetrahaem-containing quinol dehydrogenase CymA in that process. cytochrome electrochemistry haem mineral reduction quinone Shewanella...
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Biochem Soc Trans (2009) 37 (2): 408–412.
Published: 20 March 2009
...Sara A. Rafice; Nishma Chauhan; Igor Efimov; Jaswir Basran; Emma Lloyd Raven The family of haem dioxygenases catalyse the initial oxidative cleavage of L -tryptophan to N -formylkynurenine, which is the first, rate-limiting, step in the L -kynurenine pathway. In the present paper, we discuss...
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Biochem Soc Trans (2008) 36 (6): 1239–1241.
Published: 19 November 2008
... both ferric reductase activity and stimulate uptake of 59 Fe. An additional increase in cupric reductase activity was found in MDCK (Madin–Darby canine kidney) cells expressing Dcytb. Expression and purification of Dcytb in insect cells reveals that Dcytb is a di-haem protein and that the haems...
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Biochem Soc Trans (2008) 36 (6): 1120–1123.
Published: 19 November 2008
...Sarah J. Thackray; Christopher G. Mowat; Stephen K. Chapman The haem proteins TDO (tryptophan 2,3-dioxygenase) and IDO (indoleamine 2,3-dioxygenase) are specific and powerful oxidation catalysts that insert one molecule of dioxygen into L -tryptophan in the first and rate-limiting step...
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Biochem Soc Trans (2008) 36 (6): 1103–1105.
Published: 19 November 2008
... oxidase haem magnetic circular dichroism (MCD) Sitting some 60 miles south of UEA (University of East Anglia), I have watched with great admiration the growth and development of the CMSB (Centre for Metalloprotein Spectroscopy and Biology) over the past 30 years. That it has grown during...
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Biochem Soc Trans (2008) 36 (6): 1106–1111.
Published: 19 November 2008
... The Authors Journal compilation © 2008 Biochemical Society 2008 abzyme de novo protein design haem maquette protein engineering water penetration There is evidence of water exclusion even in this first haem maquette, H10H24. The reduction potential of the haem is pH-dependent and coupled...
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Biochem Soc Trans (2008) 36 (6): 1149–1154.
Published: 19 November 2008
...Brian R. Crane Mammalian NOSs (nitric oxide synthases) are haem-based monoxygenases that oxidize the amino acid arginine to the intracellular signal and protective cytotoxin nitric oxide (NO). Certain strains of mostly Gram-positive bacteria contain homologues of the mammalian NOS catalytic domain...
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Biochem Soc Trans (2008) 36 (6): 1124–1128.
Published: 19 November 2008
...Despoina A.I. Mavridou; Martin Braun; Linda Thöny-Meyer; Julie M. Stevens; Stuart J. Ferguson The CXXCH motif is usually recognized in the bacterial periplasm as a haem attachment site in apocytochromes c . There is evidence that the Escherichia coli Ccm (cytochrome c maturation) system recognizes...
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Biochem Soc Trans (2006) 34 (6): 1173–1177.
Published: 25 October 2006
... correspondence should be addressed (email Andrew.Munro@Manchester.ac.uk ). 26 6 2006 © 2006 The Biochemical Society 2006 Bacillus BM3 CYP102 electron transfer flavocytochrome haem An alignment of amino acid sequences of 15 bacterial BM3-like P450–CPR fusion enzymes demonstrates...
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Biochem Soc Trans (2006) 34 (1): 150–151.
Published: 20 January 2006
...J.W.A. Allen; S.J. Ferguson c -Type cytochromes are characterized by covalent attachment of haem to protein through thioether bonds between the vinyl groups of the haem and the thiols of a CXXCH motif. Proteins of this type play crucial roles in the biochemistry of the nitrogen cycle. Many Gram...
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Biochem Soc Trans (2005) 33 (4): 737–742.
Published: 01 August 2005
...M. Moulin; A.G. Smith Plant tetrapyrroles are the most abundant biomolecules on the earth and are cofactors of many apoproteins essential for plant function. The four end-products sirohaem, chlorophyll, haem and phytochromobilin are synthesized by a common branched pathway, which is tightly...
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Biochem Soc Trans (2005) 33 (4): 792–795.
Published: 01 August 2005
...J.M. Stevens; T. Uchida; O. Daltrop; S.J. Ferguson Haem (Fe-protoporphyrin IX) is a cofactor found in a wide variety of proteins. It confers diverse functions, including electron transfer, the binding and sensing of gases, and many types of catalysis. The majority of cofactors are non-covalently...
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Biochem Soc Trans (2005) 33 (1): 149–151.
Published: 01 February 2005
...A. Crow; N.E. Le Brun; A. Oubrie Numerous bacterial proteins involved in the nitrogen cycle, and other processes, require c -type haem as a cofactor. c -type cytochromes are formed by covalent attachment of haem to the conserved CXXCH motif. Here, we briefly review what is presently known about...
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Biochem Soc Trans (2005) 33 (1): 145–146.
Published: 01 February 2005
...J.W.A. Allen; M.L. Ginger; S.J. Ferguson c -type cytochromes contain haem covalently attached to protein by thioether bonds formed post-translationally and requiring a dedicated biogenesis apparatus. Three biogenesis systems, found in different cell types, are well known. Here we discuss emerging...
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Biochem Soc Trans (2005) 33 (1): 137–140.
Published: 01 February 2005
... 2005 Figure 1 Structural and EPR spectroscopic data of E. coli oxidized NrfA ( A , left) Overall structure of NrfA. ( A , right) Details of the active site showing conserved residues, the calcium ion and a water/hydroxide bound to haem 1. Images were produced with WebLab ViewerPro. PDB file...
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Biochem Soc Trans (2003) 31 (3): 553–557.
Published: 01 June 2003
.... It contains a 5-coordinate (5c) His-ligated haem that shares spectroscopic and ligand-binding properties with the haem group in the sensory domain of soluble guanylate cyclase (sGC). The latter is an extremely important enzyme involved in the control of vasodilation and blood clotting. Curiously, the enzyme...
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Biochem Soc Trans (2002) 30 (4): 658–662.
Published: 01 August 2002
... in bioremediation. The wide variety of respiratory substrates for Shewanella is correlated with the evolution of several multi-haem membrane-bound, periplasmic and outer-membrane c -type cytochromes. The 21 kDa c -type cytochrome CymA of the freshwater strain Shewanella oneidensis MR-1 has an N-terminal membrane...
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Biochem Soc Trans (2002) 30 (4): 579–584.
Published: 01 August 2002
... aldehyde between glutamyl-tRNA reductase and the aminomutase is proposed. 1 To whom correspondence should be addressed (e-mail d.jahn@tu-bs.de ) 13 3 2002 © 2002 Biochemical Society 2002 catalytic mechanism crystal structure haem tetrapyrrole biosynthesis ALA, 5...
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Biochem Soc Trans (2001) 29 (2): 105–111.
Published: 01 May 2001
...E. Lloyd Raven; A. Celik; P. M. Cullis; R. Sangar; M. J. Sutcliffe Understanding the catalytic versatility of haem enzymes, and in particular the relationships that exist between different classes of haem-containing proteins and the mechanisms by which the apo-protein structure controls chemical...