Structural characterization of synthetic and protein-bound porphyrins in terms of the lowest-frequency normal coordinates of the macrocycle

Journal of Physical Chemistry B

Volumn 101, Issue 9, 1997, Pages 1684-1699

  Jentzen, Walter ^a   Song, Xing Zhi ^a   Shelnutt, John A ^a  

^a NONE

Author keywords

[No Author keywords available]

Indexed keywords

ATOMS; CALCULATIONS; CHARACTERIZATION; CHEMICAL BONDS; CLASSIFICATION (OF INFORMATION); CRYSTAL STRUCTURE; LATTICE VIBRATIONS;

HEME DISTORTION; HEMOPROTEINS; MACROCYCLE; METALLOPORPHYRIN; X RAY CRYSTAL STRUCTURE;

PROTEINS;

EID: 0031078856     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp963142h     Document Type: Article

References (118)

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103. The displacements were obtained by orienting the macrocycle with its peripheral substituems according to Figure 4 (panel C). The resolution of the X-ray crystal structures and PDB reference codes are also given. Hildenb.: Desulfovibrio vulgaris, strain Hildenborough, 2.0-Å resolution, ref 65a (2CYM). Miyaz.: D. vulgaris, strain Miyazaki, 1.8-Å resolution, ref 65b (2CDV). ATCC: D. desulfuricans, strain ATCC 27 774, 1.75-Å resolution, ref 65c (2CYR). Norw.: D. desulfuricans, strain Norway, 1.7-Å resolution, ref 65d (2CY3).
104. oop,1 between the observed and simulated distortion is 0.034(19) Å for all heme groups.
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118. The total nonplanar distortions range from 0.3 to 0.8 Å, while the individual contributions vary from -0.5 to 0.6 Å for sad, -0.2 to 0.6 Å for ruf, -0.3 to 0.3 Å for dom, and -0.2 to 0.4 Å for the wav(x) and wav(y) deformations. Again, no significant pro deformation is observed because it requires a much greater expenditure of energy by the protein, and therefore much smaller deformation of this type is likely to be observed in the structures of the heme groups.