Proton transfer within the active-site cavity of carbonic anhydrase III

An, Haiqian; Tu, Cong; Ren, Ke; Laipis, Philip J.; Silverman, David N.

doi:10.1016/s0167-4838(02)00374-6

Cited by 18 publications

(29 citation statements)

References 30 publications

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“…The investigators also demonstrated that sustained off-resonance irradiation CID (SORI-CID)-the application of an electromagnetic pulse with a frequency lower than the cyclotron frequency of the protein in the presence of nitrogen gas-induced the loss of some of the ligands from the protein-ligand complex ions, in a manner that scaled with the intensity of the pulse. 445,446 The intensity of the pulse that generated equal ion intensities for the CA II-ligand complex and free CA II was termed E 50 and was used to compare the relative stabilities of different CA II-ligand complexes in the gas phase. 445,446 …”

Section: Mass Spectrometrymentioning

confidence: 99%

“…445,446 Gas-phase complex stability was estimated by the intensity of radiation (E 50 ) required to dissociate half of the CA II-ligand complex ions to unbound CA II ions; E 50 increases with increasing stability of the complex. 50 for complexes of BCA II with eight p-substituted benzenesulfonamides with short peptide tails. 445 They did not observe a clear correlation between E 50 and the hydrophobicity of the amino acid closest to the phenyl ring of the ligand, while they did observe such a correlation for the thermodynamic ( ) and kinetic stability (k off ) of the BCA II-ligand complexes in solution.…”

Section: Using Mass Spectrometry To Understand the Stability Of Protementioning

confidence: 99%

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Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein−Ligand Binding

et al. 2008

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I. Introduction to Carbonic Anhydrase (CA) and to the Review 948 1. Introduction: Overview of CA as a Model 948 1.1. Value of Models 950 1.2. Objectives and Scope of the Review 950 2. Overview of Enzymatic Activity 950 3. Medical Relevance 951 II. Structure and Structure−Function Relationships of CA 953 4. Global and Active-Site Structure 953 4.1. Structure of Isoforms 953 4.2. Isolation and Purification 954 4.3. Crystallization 954 4.4. Structures Determined by X-ray Crystallography and NMR 955 4.4.1. Structures Determined by X-ray Crystallography 955 4.4.2. Structure Determined by NMR 955 4.5. Global Structural Features 963 4.6. Structure of the Binding Cavity 964 4.7. Zn II -Bound Water 965 5. Metalloenzyme Variants 966 6. Structure−Function Relationships in the Catalytic Active Site of CA 968 6.1. Effects of Ligands Directly Bound to Zn II 968 6.2. Effects of Indirect Ligands 969 7. Physical-Organic Models of the Active Site of CA 969 III. Using CA as a Model to Study Protein−Ligand Binding 970 8. Assays for Measuring Thermodynamic and Kinetic Parameters for Binding of Substrates and Inhibitors 970 8.1. Overview 970 8.

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Section: Mass Spectrometrymentioning

confidence: 99%

Section: Using Mass Spectrometry To Understand the Stability Of Protementioning

confidence: 99%

Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein−Ligand Binding

et al. 2008

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“…45 In CAIII, three histidine residues at different positions 64, 67 and 131 are replaced by Lys64, Arg67 and Phe131, and these are found to be key residues for protons transfer during catalysis. 46 Interestingly, in CAIV a dramatic decrease in the activity was observed if the Gly63 was mutated to Gln, because this site was present in vicinity of His64. 47 Moreover, CAVA has Tyr64 as proton shuttle, instead of most conserved His64 48 , and its catalytic proton transfer activity is distressed by the bulky side of Phe66 (Fig.…”

Section: Primary and Secondary Structurementioning

confidence: 99%

Structure, function and applications of carbonic anhydrase isozymes

Hassan

Shajee

Waheed

et al. 2013

Bioorganic & Medicinal Chemistry

224

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“…The underlying cause for this is the major differences in the active site region of the enzyme: the presence of Lys64 and Phe198 in CA III. CA II contains a His residue in position 64, which is much more effective as a proton shuttle than Lys residue 45,46 . In order to regenerate the basic form of the enzyme from the catalytically inactive form, a proton transfer reaction takes place 2 .…”

Section: Structure and Function Of Ca IIImentioning

confidence: 99%