Reversible Binding of a Protein to a Ligand: Oxygen-Binding Proteins:- Hemoglobin Undergoes a Structural Change on Binding Oxygen

X-ray analysis has revealed two major conformations of hemoglobin: the R state and the T state. Although oxy gen binds to hemoglobin in either state, it has a significantly higher affinity for hemoglobin in the R state. Oxy gen binding stabilizes the R state. When oxygen is absent experimentally, the T state is more stable and is thus the predominant conformation of deoxyhemoglobin. T and R originally denoted “tense” and “relaxed,” respectively, because the T state is stabilized by a greater number of ion pairs, many of which lie at the α₁β₂ (and α₂β₁) interfaces (Fig. 5–9). The binding of O₂ to a hemoglobin subunit in the T state triggers a change in conformation to the R state. When the entire protein undergoes this transition, the structures of the individual subunits change little, but the αβ subunit pairs slide past each other and rotate, narrowing the pocket between the subunits (Fig. 5–10). In this process, some of the ion pairs that stabilize the T state are broken and some new ones are formed. Max Perutz proposed that the T → R transition is triggered by changes in the positions of key amino acid side chains surrounding the heme. In the T state, the porphyrin is slightly puckered, causing the heme iron to protrude somewhat on the proximal His (His F8) side. The binding of O₂ causes the heme to assume a more planar conformation, shifting the position of the proximal His and the attached F helix (Fig. 5–11). These changes lead to adjustments in the ion pairs at the α₁β₂ interface.

FIGURE 5–9 Some ion pairs that stabilize the T state of deoxyhe moglobin. (a) A close-up view of a portion of a deoxyhemoglobin molecule in the T state (PDB ID 1HGA). Interactions between the ion pairs His HC3 and Asp FG1 of the subunit (blue) and between Lys C5 of the α subunit (gray) and His HC3 (its -carboxyl group) of the β subunit are shown with dashed lines. (Recall that HC3 is the carboxyl-terminal residue of the β subunit.) (b) The interactions between these ion pairs, and between others not shown in (a), are schematized in this representation of the extended polypeptide chains of hemoglobin.

FIGURE 5–10 The T→R transition. (PDB ID 1HGA and 1BBB) In these depictions of deoxyhemoglobin, as in Figure 5–9, the β subunits are blue and the α subunits are gray. Positively charged side chains and chain termini involved in ion pairs are shown in blue, their negatively charged partners in red. The Lys C5 of each α subunit and Asp FG1 of each β subunit are visible but not labeled (compare Fig. 5–9a). Note that the molecule is oriented slightly differently than in Figure 5–9. The transition from the T state to the R state shifts the subunit pairs substantially, affecting certain ion pairs. Most noticeably, the His HC3 residues at the carboxyl termini of the subunits, which are in volved in ion pairs in the T state, rotate in the R state toward the center of the molecule, where they are no longer in ion pairs. Another dramatic result of the T → R transition is a narrowing of the pocket between the β subunits.

اخر الاخبار

اخبار العتبة العباسية المقدسة

قسم التطوير يقدم دورة عن أخلاقيات المهنة ضمن برنامج تأهيل المنتسبين الجدد

ضمن برنامج (وفاءً للدماء).. المجمع العلمي يقيم محفلًا قرآنيًّا في محافظة المثنى

قسم الشؤون الفكرية يرفد المكتبة المركزية في ديالى بإصدارات معرفية

قسم التطوير يبحث مع ديوان الوقف الشيعي آفاق التعاون في مجال التدريب والتطوير المؤسسي

المزيد

الآخبار الصحية

المركز الاوروبي : كل ركاب سفينة "هانتا" مخالطون معرضون لخطر كبير

ألمانيا.. رئيس الأطباء يدعو للإسراع بتطبيق "ضريبة السكر"

بين الفائدة والضرر.. جدل حول تأثير الشاي والقهوة على العظام

أمراض خطيرة.. أبحاث تكشف مخاطر الجلوس لفترة طويلة

المزيد

الآخبار التكنلوجية

سبع حقائق غير متوقعة عن موجات الراديو

الأجسام الغريبة.. ماذا رأى رواد "أبولو 17" على القمر؟

حرارة المحيطات عند مستويات مقلقة.. وعودة "إل نينيو" تقترب

باحثون يحددون تأثير القهوة على الميكروبيوم والمزاج

المزيد

مواضيع ذات صلة

Reversible Binding of a Protein to a Ligand: Oxygen-Binding Proteins:- Cooperative Ligand Binding Can Be Described

Reversible Binding of a Protein to a Ligand: Oxygen-Binding Proteins:- Hemoglobin Subunits Are Structurally Similar to Myoglobin

Reversible Binding of a Protein to a Ligand: Oxygen-Binding Proteins: -Oxygen Is Transported in Blood by Hemoglobin

Reversible Binding of a Protein to a Ligand: Oxygen-Binding Proteins:- Protein Structure Affects How Ligands Bind

Membrane Dynamics:- Transbilayer Movement of Lipids Requires Catalysis

The Composition and Architecture of Membranes:- Lipids and Proteins Diffuse Laterally in the Bilayer

Membrane Dynamics:- Acyl Groups in the Bilayer Interior Are Ordered to Varying Degrees

The Composition and Architecture of Membranes:- Covalently Attached Lipids Anchor Some Membrane Proteins

The Composition and Architecture of Membranes:- The Topology of an Integral Membrane Protein Can Be Predicted from Its Sequence

The Composition and Architecture of Membranes: -Integral Proteins Are Held in the Membrane by Hydrophobic Interactions with Lipids

The Composition and Architecture of Membranes:- All Biological Membranes Share Some Fundamental Properties

The Composition and Architecture of Membranes:- Each Type of Membrane Has Characteristic Lipids and Proteins