Metal-activated histidine carbon donor hydrogen bonds contribute to metalloprotein folding and function

Ann Schmiedekamp, Vikas Nanda

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Carbon donor hydrogen bonds are typically weak interactions that contribute less than 2 kcal/mol, and provide only modest stabilization in proteins. One exception is the class of hydrogen bonds donated by heterocyclic side chain carbons. Histidine is capable of particularly strong interactions through the Cε1 and Cδ2 carbons when the imidazole is protonated or bound to metal. Given the frequent occurrence of metal-bound histidines in metalloproteins, we characterized the energies of these interactions through DFT calculations on model compounds. Imidazole-water hydrogen bonding could vary from -11.0 to -17.0 kcal/mol, depending on the metal identity and oxidation state. A geometric search of metalloprotein structures in the PDB identified a number of candidate His C-H···O hydrogen bonds which may be important for folding or function. DFT calculations on model complexes of superoxide reductase show a carbon donor hydrogen bond positioning a water molecule above the active site.

Original languageEnglish (US)
Pages (from-to)1054-1060
Number of pages7
JournalJournal of Inorganic Biochemistry
Volume103
Issue number7
DOIs
StatePublished - Jul 1 2009

Fingerprint

Metalloproteins
Histidine
Activated carbon
Hydrogen
Hydrogen bonds
Carbon
Metals
Discrete Fourier transforms
Water
Hydrogen Bonding
Catalytic Domain
Stabilization
Oxidation
Molecules
Proteins
imidazole

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Inorganic Chemistry

Cite this

@article{e54c97f32633472dac1fa1b195520d60,
title = "Metal-activated histidine carbon donor hydrogen bonds contribute to metalloprotein folding and function",
abstract = "Carbon donor hydrogen bonds are typically weak interactions that contribute less than 2 kcal/mol, and provide only modest stabilization in proteins. One exception is the class of hydrogen bonds donated by heterocyclic side chain carbons. Histidine is capable of particularly strong interactions through the Cε1 and Cδ2 carbons when the imidazole is protonated or bound to metal. Given the frequent occurrence of metal-bound histidines in metalloproteins, we characterized the energies of these interactions through DFT calculations on model compounds. Imidazole-water hydrogen bonding could vary from -11.0 to -17.0 kcal/mol, depending on the metal identity and oxidation state. A geometric search of metalloprotein structures in the PDB identified a number of candidate His C-H···O hydrogen bonds which may be important for folding or function. DFT calculations on model complexes of superoxide reductase show a carbon donor hydrogen bond positioning a water molecule above the active site.",
author = "Ann Schmiedekamp and Vikas Nanda",
year = "2009",
month = "7",
day = "1",
doi = "10.1016/j.jinorgbio.2009.04.017",
language = "English (US)",
volume = "103",
pages = "1054--1060",
journal = "Journal of Inorganic Biochemistry",
issn = "0162-0134",
publisher = "Elsevier Inc.",
number = "7",

}

Metal-activated histidine carbon donor hydrogen bonds contribute to metalloprotein folding and function. / Schmiedekamp, Ann; Nanda, Vikas.

In: Journal of Inorganic Biochemistry, Vol. 103, No. 7, 01.07.2009, p. 1054-1060.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Metal-activated histidine carbon donor hydrogen bonds contribute to metalloprotein folding and function

AU - Schmiedekamp, Ann

AU - Nanda, Vikas

PY - 2009/7/1

Y1 - 2009/7/1

N2 - Carbon donor hydrogen bonds are typically weak interactions that contribute less than 2 kcal/mol, and provide only modest stabilization in proteins. One exception is the class of hydrogen bonds donated by heterocyclic side chain carbons. Histidine is capable of particularly strong interactions through the Cε1 and Cδ2 carbons when the imidazole is protonated or bound to metal. Given the frequent occurrence of metal-bound histidines in metalloproteins, we characterized the energies of these interactions through DFT calculations on model compounds. Imidazole-water hydrogen bonding could vary from -11.0 to -17.0 kcal/mol, depending on the metal identity and oxidation state. A geometric search of metalloprotein structures in the PDB identified a number of candidate His C-H···O hydrogen bonds which may be important for folding or function. DFT calculations on model complexes of superoxide reductase show a carbon donor hydrogen bond positioning a water molecule above the active site.

AB - Carbon donor hydrogen bonds are typically weak interactions that contribute less than 2 kcal/mol, and provide only modest stabilization in proteins. One exception is the class of hydrogen bonds donated by heterocyclic side chain carbons. Histidine is capable of particularly strong interactions through the Cε1 and Cδ2 carbons when the imidazole is protonated or bound to metal. Given the frequent occurrence of metal-bound histidines in metalloproteins, we characterized the energies of these interactions through DFT calculations on model compounds. Imidazole-water hydrogen bonding could vary from -11.0 to -17.0 kcal/mol, depending on the metal identity and oxidation state. A geometric search of metalloprotein structures in the PDB identified a number of candidate His C-H···O hydrogen bonds which may be important for folding or function. DFT calculations on model complexes of superoxide reductase show a carbon donor hydrogen bond positioning a water molecule above the active site.

UR - http://www.scopus.com/inward/record.url?scp=67449113526&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=67449113526&partnerID=8YFLogxK

U2 - 10.1016/j.jinorgbio.2009.04.017

DO - 10.1016/j.jinorgbio.2009.04.017

M3 - Article

C2 - 19501913

AN - SCOPUS:67449113526

VL - 103

SP - 1054

EP - 1060

JO - Journal of Inorganic Biochemistry

JF - Journal of Inorganic Biochemistry

SN - 0162-0134

IS - 7

ER -