32-38There has been a renewed interest in understanding the function of hemoglobins in recent years because of their diverse cellular locations and unique physical properties. Although the non vertebrate hemoglobins bind dioxygen and other ligands just as the vertebrate hemoglobins, the kinetic and structural properties of the oxygen complexes differ significantly suggesting functional diversity. This paper describes our recent work on a series of nonvertebrate hemoglobins using state-of the- art resonance Raman spectroscopy with the aim of deciphering various biological oxygen utilization mechanisms
Resonance Raman (RR) spectroscopy is potentially one of the most effective methods to investigate th...
The Heme-Nitric oxide/OXygen binding (H-NOX) domain encompasses a family of proteins closely related...
The interaction of molecular oxygen (O(,2)) with metalloporphyrins has intrigued scientists of many ...
Heme proteins, which are ubiquitous in physiological systems, are key components involved in many bi...
Heme proteins are a well-studied class of enzymes capable of varied catalytic function. Some of the ...
Hemoglobin (Hb) is a key component of respiratory system and as such plays important role in human p...
Resonance Raman spectroscopy is now well established as a powerful structural probe of heme proteins...
Resonance Raman spectra from intact viable erythrocytes can be used to study oxygen uptake in soluti...
The molecular mechanism of O2 binding to hemoglobin (Hb) and myoglobin (Mb) is a long-standing issue...
The substitution of iron for cobalt in the monomeric insect hemoglobin CTT (Chironomus thummi thummi...
Heme proteins are ubiquitous in nature and they are involved in different biochemical processes: oxy...
Photoinduced oxygen dynamics in hemoglobin is monitored by surface enhanced resonant Raman spectrosc...
The interaction of molecular oxygen (O(,2)) with metalloporphyrins has intrigued scientists of many ...
In the past two decades a number spectroscopic techniques and physicochemical measurements have been...
Hemoglobin (Hb) is an essential component of the circulatory system of vertebrates. Its chief physio...
Resonance Raman (RR) spectroscopy is potentially one of the most effective methods to investigate th...
The Heme-Nitric oxide/OXygen binding (H-NOX) domain encompasses a family of proteins closely related...
The interaction of molecular oxygen (O(,2)) with metalloporphyrins has intrigued scientists of many ...
Heme proteins, which are ubiquitous in physiological systems, are key components involved in many bi...
Heme proteins are a well-studied class of enzymes capable of varied catalytic function. Some of the ...
Hemoglobin (Hb) is a key component of respiratory system and as such plays important role in human p...
Resonance Raman spectroscopy is now well established as a powerful structural probe of heme proteins...
Resonance Raman spectra from intact viable erythrocytes can be used to study oxygen uptake in soluti...
The molecular mechanism of O2 binding to hemoglobin (Hb) and myoglobin (Mb) is a long-standing issue...
The substitution of iron for cobalt in the monomeric insect hemoglobin CTT (Chironomus thummi thummi...
Heme proteins are ubiquitous in nature and they are involved in different biochemical processes: oxy...
Photoinduced oxygen dynamics in hemoglobin is monitored by surface enhanced resonant Raman spectrosc...
The interaction of molecular oxygen (O(,2)) with metalloporphyrins has intrigued scientists of many ...
In the past two decades a number spectroscopic techniques and physicochemical measurements have been...
Hemoglobin (Hb) is an essential component of the circulatory system of vertebrates. Its chief physio...
Resonance Raman (RR) spectroscopy is potentially one of the most effective methods to investigate th...
The Heme-Nitric oxide/OXygen binding (H-NOX) domain encompasses a family of proteins closely related...
The interaction of molecular oxygen (O(,2)) with metalloporphyrins has intrigued scientists of many ...