|Table of Contents|

Fluorescence Spectra Assignment of Domains in Pig Cardiac Metmyoglobin Under Energy Excitation(PDF)

《南京师大学报（自然科学版）》[ISSN:1001-4616/CN:32-1239/N]

Issue:
2015年02期
Page:
59-
Research Field:
化学
Publishing date:

Info

Title:
Fluorescence Spectra Assignment of Domains in Pig Cardiac Metmyoglobin Under Energy Excitation
Author(s):
Wu Mingcao1; Jin Bangquan1; Feng Yuying2; Chen Xuming1; Huang Heyong2
(1.Department of Food Science and Nutrition,Nanjing Normal University,Nanjing 210097,China) (2.Analysis and Testing Center,Nanjing 210023,China)
Keywords:
domains; Heme-Fe3+; electron and energy transition; pig cardiac metmyoglobin; fluorescence spectra
PACS:
S828
DOI:
-
Abstract:
Purified pig cardiac metmyoglobin(pMetMb)was used to study its functional domains under the suitable fluorescence conditions. When 600 nm/min scanning speed and the medium response time were set up,the optimal fluorescence conditions for pMetMb spontaneous(emission)fluorescence were 20 mmol/L pMetMb,10 nm slit width with 270 nm or 430 nm excitation wavelength,respectively. By the resolve of the synchronous fluorescence spectra,the domains of tyrosine(Tyr),tryptophan(Trp)residue and heme-Fe3+ group were located at 312 nm,355 nm and 630 nm,respectively. Those were their special emission peaks of fluorescence spectra. 270 nm was the optimal excitation wavelength for Tyr and Trp residues,while 430 nm was optimal for heme-Fe3+ group. At those locations their powerful spontaneous fluorescence spectra were found. Compared with horse myoglobin(hMb-heme-Fe2+),the Trp residue and heme-Fe3+fluorescence spectra of pMetMb appeared as redshift from 595 nm to 630 nm. The results also showed that if excitation wavelength was far away from another molecule(as 270 nm for heme-Fe3+ group),spontaneous fluorescence was quenched without inducing clearly electron transfer and energy transition. However in a short-distance,a 430 nm excitation wavelength could induce the fluorescence emission of heme-Fe3+ group at 630 nm mostly. In a summary,it was suggested that high-spin pentacoordination of Mb-heme-Fe2+ was changed into low-spin hexacoordination of MetMb-heme-Fe3+.

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Last Update: 2015-06-30