Cupric ion complexes of histidine-containing peptides.

نویسندگان

  • G F Bryce
  • R W Roeske
  • F R Gurd
چکیده

The binding of cupric or zinc ion by sperm whale metmyoglobin appears to involve imidazole groups of histidyl residues (4, 5) that occur well removed from the NH2 terminus (6). The binding of each cupric ion by metmyoglobin is accompanied on the average by the displacement of one or more protons beyond that that may be borne by the imidazole group, presumably from peptide amide nitrogen atoms (4, 5). Such displacement of amide protons is best known for simple peptides containing a free terminal amino group (1, 7-10). Histidine-containing peptides lacking a free terminal amino group have been studied very little, except for one in which flexibility is probably quite restricted (11). For these reasons, the observations with metmyoglobin have remained unparalleled with model peptide systems (4, 12). The present paper deals with complex formation between cupric ions and a number of histidine-containing peptides including a series of peptides of the form acetyl(glycyl),-L-histidine, acetylglycyl-L-histidylglycine, and some of the corresponding peptides lacking the terminal acetyl group. The results show that the longer acetylated histidine-containing peptides react with cupric ions to form 1:l complexes that dissociate protons in comparable number and in a comparable pH range to the cupric ion complexes of metmyoglobin or apomyoglobin.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Optical rotatory properties of cupric ion complexes of simple dipeptides.

Titrations and spectral measurements of sperm whale metmyoglobin (2) and apomyoglobin (3) in the presence of cupric ion indicate that the metal ion may form chelates with imidazole groups and some other proton-bearing groups such as peptide amides. The titration and spectral properties of complexes of certain histidine-containing peptides have proved to be similar to those of the protein (4). A...

متن کامل

ESEEM Analysis of Multi-Histidine Cu(II)-Coordination in Model Complexes, Peptides, and Amyloid-β

We validate the use of ESEEM to predict the number of (14)N nuclei coupled to a Cu(II) ion by the use of model complexes and two small peptides with well-known Cu(II) coordination. We apply this method to gain new insight into less explored aspects of Cu(II) coordination in amyloid-β (Aβ). Aβ has two coordination modes of Cu(II) at physiological pH. A controversy has existed regarding the numbe...

متن کامل

L-histidine-containing peptides as models for the interaction of copper (II) and nickel (II) ions with sperm whale apomyoglobin.

1. The association and ionization constants for nickel (II) and a selection of L-histidine-containing peptides have been computed together with the constants for copper (II) and acetylglycylglycyl-L-histidylglycine. 2. A close parallel between the titration behavior of copper (II) apomyoglobin complexes and model peptides has been obtained on the assumption that 1 of the 4 bound metal ions is s...

متن کامل

Studies on Nickel(II)-Pyridoxamine-Imidazole Containing Mixed Ligand Complex Systems

The stability constants of species present in the systems Ni(II)-pyridoxamine(pym)(A) and Ni(II)-pyridoxamine(pym)(A)-imidazole containing ligands(B) [B = imidazole(him),  benzimidazole(bim), histamine(hist) and L-histidine(his)] have been determined pH-metrically using the MINIQUAD computer program. The existence of the species NiAH, NiA and NiA2 was proven for the Ni(II)-pym(A)...

متن کامل

Modeling Cu(II) Binding to Peptides Using the Extensible Systematic Force Field

The utility of the extensible systematic force field (ESFF) was tested for copper(II) binding to a 34-amino-acid Cu(II) peptide, which includes five histidine residues and is the putative copper-binding site of lysyl oxidase. To improve computational efficiency, distance geometry calculations were used to constrain all combinations of three histidine ligands to be within bonding distance of the...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 240 10  شماره 

صفحات  -

تاریخ انتشار 1965