Guest Penetration Deep within the Cavity of Calix[4]arene Hosts: The Tight Binding of Nitric Oxide to Distal (Cofacial) Aromatic Groups

Rathore, Rajendra; Lindeman, Sergey V.; Rao, K. S. S. P.; Sun, Duoli; Kochi, Jay K.

doi:10.1002/1521-3773(20000616)39:12<2123::aid-anie2123>3.0.co;2-4

Cited by 78 publications

(71 citation statements)

References 32 publications

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“…The precise nature of such sites remains elusive, but aromatic residues are attractive possible components. The ability of aromatic ring structures to bind NO, tightly and reversibly, is shown unequivocally by the NO binding between the cofacial aromatic groups of so-called "Venus fly trap" organic compounds recently reported by Kochi and co-workers (45,46). The ability to detect NNO at different sites within protein by IR spectroscopy, coupled with the evidence found in support of NO and NNO binding at the same sites, illustrate the utility of NNO-IR spectroscopy for detecting potential nonmetal sites for NO binding via noncovalent bonding.…”

Section: Discussionmentioning

confidence: 99%

Anesthetic-like Interactions of Nitric Oxide with Albumin and Hemeproteins

Sampath¹,

Zhao²,

Caughey³

2001

Journal of Biological Chemistry

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The mechanisms of anesthesia and the regulatory functions of nitric oxide (NO) 1 remain far from clear. Potential roles of anesthetic-protein interactions in anesthesia have become of increasing interest (1-5) as have the interactions of NO with proteins (6 -10). Volatile anesthetics occupy hydrophobic sites within protein without formation of covalent bonds with amino acid residues. In contrast, the reactions between NO and receptor sites in proteins that have been studied extensively involve covalent bond formation, as in metal nitrosyl and Snitrosothiol (-SNO) derivatives (7-10). Nitrosations (i.e. attack of protein residues by NOϩ) on exposure of proteins to NO with a suitable oxidant present are the only reactions of NO that have been discussed other than the binding of NO to metal sites. Evidence of NO occupying sites within proteins as an uncharged diatomic free radical by means of anesthetic-like noncovalent bonding has not been reported.The binding of volatile anesthetics to serum albumins and the effects of such binding on protein structure are considered in several recent reports. Specific, saturable binding of halothane and other anesthetics to bovine serum albumin and anesthetic-induced alterations in the structure or carrier function of this protein have been shown (11-16). The anesthetic nitrous oxide (NNO) was detected at sites within human serum albumin (HSA) (5). Infrared (IR) spectra of bound NNO molecules demonstrated sites of two types. The exposure of HSA to NNO enhanced absorbance in the S-H stretching region of the IR spectrum giving evidence of an NNO-induced change in protein conformation near Cys 34 (5). In 1992, NO was proposed to circulate in mammalian plasma primarily in association with serum albumin, due to formation of the S-nitrosothiol derivative (17). However, the similarities in the structure and physical properties of NNO and NO suggest the possibility that NO may also interact at some sites within albumin in the manner shown for NNO.IR evidence of NNO molecules at multiple sites within hemoglobin, myoglobin, and cytochrome c oxidase (CcO) has also been obtained (5,18). NNO neither serves as a ligand to heme iron nor reacts with thiols. The ability of NNO to alter hemeprotein structure and function was shown by shifts in the IR spectra of cysteine thiols of HbA (5) and by partial and reversible inhibitions of CcO (18). The well established ability of NO to ligate to heme iron in HbA, Mb, and CcO, and to copper B in CcO (19,20), led to the assumption of metal binding in proposed mechanisms for physiologically important reactions of NO with hemeproteins. Reactions of NO with HbA that result in S-nitrosothiol derivative formation have also received much attention (8). However, alternative mechanisms whereby NO alters hemeprotein structure and function by noncovalent anesthetic-like bonding to sites that involve neither metal nor cysteine sulfur remain unexplored.Much interest in possible physiological roles of carbon monoxide (CO), including a messenger role in the nervous syst...

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Section: Discussionmentioning

confidence: 99%

Anesthetic-like Interactions of Nitric Oxide with Albumin and Hemeproteins

Sampath¹,

Zhao²,

Caughey³

2001

Journal of Biological Chemistry

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“…In addition, it has recently been shown that NO ⅐ may also occupy noncovalent binding sites in hemoglobin (8). In analogy to a synthetic model in which NO ⅐ is bound tightly and reversibly between two cofacial aromatic groups (71,72), it is conceivable that NO ⅐ may be trapped in hemoglobin by aromatic amino acid residues (8). Interestingly, two aromatic amino acids, Tyr-␤145 and Phe-␤103, are located at a distance of 4 -5 Å from the sulfur atom of Cys-␤93 and could thus facilitate noncovalent NO ⅐ binding.…”

Section: Discussionmentioning

confidence: 99%

Reactions of Deoxy-, Oxy-, and Methemoglobin with Nitrogen Monoxide

Herold

Röck

2003

Journal of Biological Chemistry

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The reaction between hemoglobin (Hb) and NO ⅐ has been investigated thoroughly in recent years, but its mechanism is still a matter of substantial controversy. We have carried out a systematic study of the influence of the following factors on the yield of S-nitrosohemoglobin (SNO-Hb) generated from the reaction of NO ⅐ with oxy-, deoxy-, and metHb: 1) the volumetric ratio of the protein and the NO ⅐ solutions; 2) the rate of addition of the NO ⅐ solution to the protein solution; 3) the amount of NO ⅐ added; and 4) the concentration of the phosphate buffer. Our results suggest that the highest SNO-Hb yields are mostly obtained by very slow addition of substoichiometric amounts of NO ⅐ from a diluted solution. Possible pathways of SNO-Hb formation from the reaction of NO ⅐ with oxy-, deoxy-, and metHb are described. Our data strongly suggest that, because of mixing artifacts, care should be taken to use results from in vitro experiments to draw conclusion on the mechanism of the reaction in vivo.

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“…A corresponding sodium complex including toluene in the crystal structure shows a cone conformation (Bott et al, 1986). A complex containing an aluminium alkyl species (Bott et al, 1987) and a solvated complex with a nitrosyl compound (Rathore et al, 2000) have also been reported. For the synthesis of the compound, see: Bitter et al (1995).…”

Section: Related Literaturementioning

confidence: 95%

5,11,17,23-Tetra-tert-butyl-25,26,27,28-tetramethoxycalix[4]arene tetrahydrofuran solvate

et al. 2007

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Key indicators: single-crystal X-ray study; T = 153 K; mean (C-C) = 0.005 Å; disorder in main residue; R factor = 0.067; wR factor = 0.215; data-to-parameter ratio = 17.4.The asymmetric unit of the title compound, C 44 H 64 O 4 ÁC 4 H 8 O, comprises two crystallographically independent calixarene molecules, which display a partial cone conformation, and two tetrahydrofuran molecules. The crystal packing is stabilized by C-HÁ Á Á contacts involving the methoxy groups, while the solvent molecules are located in voids between the calixarene molecules. Two of the tert-butyl residues of each calixarene Related literatureThe solvent-free title compound has been described as adopting the paco-conformation (Grootenhuis et al., 1990). A corresponding sodium complex including toluene in the crystal structure shows a cone conformation (Bott et al., 1986). A complex containing an aluminium alkyl species (Bott et al., 1987)

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Guest Penetration Deep within the Cavity of Calix[4]arene Hosts: The Tight Binding of Nitric Oxide to Distal (Cofacial) Aromatic Groups

Cited by 78 publications

References 32 publications

Anesthetic-like Interactions of Nitric Oxide with Albumin and Hemeproteins

Anesthetic-like Interactions of Nitric Oxide with Albumin and Hemeproteins

Reactions of Deoxy-, Oxy-, and Methemoglobin with Nitrogen Monoxide

5,11,17,23-Tetra-tert-butyl-25,26,27,28-tetramethoxycalix[4]arene tetrahydrofuran solvate

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