ライフサイエンスコーパス: corrin

1 raction mechanisms that convert porphyrin to corrin.

2 he current views concerning the evolution of corrins.

3 e 26-kDa polypeptide at a molar ratio of 1.1 corrin/26-kDa polypeptide.

4 idistant between the hydrogenation levels of corrin and corrole, is enantiomeric, and contains two ge

5 nstrate straightforward applicability of the corrin-based chemosensor, aquacyanocobyrinic acid (ACCA)

6 theory (TD-DFT) calculations indicates that corrin-based pi --> pi transitions, which dominate the C

7 with the same avidity as observed with other corrin biosynthetic transmethylases.

8 n the literature based on lipophilic Co(III)-corrin complexes, allowing the new nitrite electrodes to

9 -deoxyadenosine and attachment of 1 equiv of corrin covalently to an active-site cysteine residue of

10 d rotation of the Ado ligand relative to the corrin gave rise to four locally minimum structures with

11 bound to RNR and 0.25 equiv of a cobalt(III) corrin is tightly associated, likely through a covalent

12 Proteolysis of corrin-labeled RTPR with endoproteinase Glu-C and peptid

13 l revealed a conspicuously better fit of the corrin ligand for Rh(III) than for Co(III) , challenging

14 D spectra suggest the cobalt exists as a non-corrin low-spin Co3+ ion in a tetragonally-distorted oct

15 attached to one of the pyrrole rings of the corrin macrocycle via an aminopropanol moiety.

16 d that, during anaerobic biosynthesis of the corrin macrocycle, the two-carbon fragment excised from

17 ts favorable orientation with respect to the corrin macrocycle, which minimizes steric repulsion duri

18 hlorovinylcobalamin models also involves the corrin pi* orbital, but reduction of the base-off dichlo

19 00 nm) assigned to Co 3d --> 3d or Co 3d --> corrin pi* transitions and by visible absorption bands s

20 d by visible absorption bands similar to the corrin pi-->pi* transitions observed for ground state Cb

21 zation of the Co 3d orbitals relative to the corrin pi/pi*-based molecular orbitals when Co2+ Cbl is

22 The second set is assigned to the corrin ring (14)N nuclei.

23 on is eliminated by placing that face of the corrin ring adjacent to a cluster of bulky hydrophobic s

24 actions with the e- and f-side chains of the corrin ring and is conserved in corrinoid-binding protei

25 of the 1-amino-2-propanol side chain of the corrin ring and the subsequent attachment of GMP to form

26 eveal that many of the interactions with the corrin ring are conserved among the human Cbl transporte

27 obalamin is sensitive to modification of the corrin ring b-propionamide of cyanocobalamin.

28 mide-phosphate, the last step of the de novo corrin ring biosynthetic branch of the adenosylcobalamin

29 ity to salvage cobyric acid (Cby), a de novo corrin ring biosynthetic intermediate, under aerobic gro

30 (encoding an essential enzyme of the de novo corrin ring biosynthetic pathway) resulted in a strain o

31 the environment around the alpha face of the corrin ring consists of bulky hydrophobic residues.

32 Two pathways for corrin ring formation have been found-an aerobic pathway

33 linkage between the nucleotide loop and the corrin ring in cobalamin.

34 The corrin ring is considerably flatter than that of AdoCbl,

35 The corrin ring is oriented such that the cobalt atom is loc

36 Although the corrin ring of vitamin B12 is unable to efficiently abso

37 e bacterium Salmonella enterica produces the corrin ring only under anaerobic conditions, but it can

38 nt intermediate state can be attributed to a corrin ring pi to Co 3d(z2) ligand to metal charge trans

39 ne another since electron attachment is to a corrin ring pi-orbital, whose energy is relatively unaff

40 m bond on a 110 fs time scale is followed by corrin ring relaxation on a 260 fs time scale.

41 Thus, the equatorial corrin ring sterically impedes binding, making Co(II)Cbi

42 the protein and the polar side chains of the corrin ring which accounts for the broad specificity of

43 -ordination bonds with the cobalt ion of the corrin ring.

44 pproximately 70 degrees to the normal of the corrin ring.

45 ions between (Z)-chloro substituents and the corrin ring.

46 llates from perpendicular to parallel to the corrin ring.

47 on the Ado group and to a lesser extent the corrin ring.

48 nd the Ade is virtually perpendicular to the corrin ring; in the minor conformer, the Ade is tilted d

49 lbenzimidazole nucleotide substituent of the corrin ring; when methylcobalamin binds to methionine sy

50 synthesis relates to its distinctive cobalt corrin structure, which is essential for B12 biochemistr