ChemInform Abstract: EUROPIUM AS A FLUORESCENT PROBE OF METAL BINDING SITES ON TRANSFER RIBONUCLEIC ACID PART 1, BINDING TO ESCHERICHIA COLI FORMYLMETHIONINE TRANSFER RIBONUCLEIC ACID

1974 ◽  
Vol 5 (31) ◽  
Author(s):  
J. M. WOLFSON ◽  
D. R. KEARNS
1994 ◽  
Vol 300 (2) ◽  
pp. 373-381 ◽  
Author(s):  
P Spencer ◽  
P M Jordan

Two distinct metal-binding sites, termed alpha and beta, have been characterized in 5-aminolaevulinic acid dehydratase from Escherichia coli. The alpha-site binds a Zn2+ ion that is essential for catalytic activity. This site can also utilize other metal ions able to function as a Lewis acid in the reaction mechanism, such as Mg2+ or Co2+. The beta-site is exclusively a transition-metal-ion-binding site thought to be involved in protein conformation, although a metal bound at this site only appears to be essential for activity if Mg2+ is to be bound at the alpha-site. The alpha- and beta-sites may be distinguished from one another by their different abilities to bind divalent-metal ions at different pH values. The occupancy of the beta-site with Zn2+ results in a decrease of protein fluorescence at pH 6. Occupancy of the alpha- and beta-sites with Co2+ results in u.v.-visible spectral changes. Spectroscopic studies with Co2+ have tentatively identified three cysteine residues at the beta-site and one at the alpha-site. Reaction with N-ethyl[14C]maleimide preferentially labels cysteine-130 at the alpha-site when Co2+ occupies the beta-site.


FEBS Letters ◽  
1996 ◽  
Vol 399 (1-2) ◽  
pp. 99-102 ◽  
Author(s):  
Svetlana Avaeva ◽  
Pavel Ignatov ◽  
Svetlana Kurilova ◽  
Tatjana Nazarova ◽  
Elena Rodina ◽  
...  

2010 ◽  
Vol 48 (6) ◽  
pp. 829-835 ◽  
Author(s):  
Bo-Young Yun ◽  
Yongbin Xu ◽  
Shunfu Piao ◽  
Nahee Kim ◽  
Jeong-Hyun Yoon ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document